|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1-489 |
0e+00 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 964.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 1 MWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA 80
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 GDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLG 160
Cdd:cd05928 121 SDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 LKAKMDAG-WTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 239
Cdd:cd05928 201 LGLKVNGRyWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRML 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 240 LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDK 319
Cdd:cd05928 281 VQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 320 GNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEV 399
Cdd:cd05928 361 GNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 400 ENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 479
Cdd:cd05928 441 ESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKI 520
|
490
....*....|
gi 815659680 480 QRAKLRDKEW 489
Cdd:cd05928 521 QRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2-486 |
0e+00 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 670.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 81
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSySSLGL 161
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDA-GWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL 240
Cdd:cd05972 108 GHIPTAaYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 241 QQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKG 320
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 321 NVLPPGTEGDIGIRVKpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVE 400
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 401 NALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQ 480
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 815659680 481 RAKLRD 486
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2-489 |
7.30e-167 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 483.07 E-value: 7.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:COG0365 40 LTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVI---------QEVDTVASECPSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGL 148
Cdd:COG0365 119 DGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 149 PKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGWI---LNILCSlmePWALGACTFVH-LLPKF-DPLVILKTLS 222
Cdd:COG0365 199 PKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGWAtghSYIVYG---PLLNGATVVLYeGRPDFpDPGRLWELIE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 SYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TM 297
Cdd:COG0365 276 KYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETG-GIFISNlpGL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 298 KIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPiRPiGIFSGYVDNPDKTAANIRGDF---WLLGDRGIKDED 374
Cdd:COG0365 355 PVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-GP-WP-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDED 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 375 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKS 454
Cdd:COG0365 432 GYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVRE 509
|
490 500 510
....*....|....*....|....*....|....*
gi 815659680 455 VTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 489
Cdd:COG0365 510 ELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
4-488 |
2.00e-159 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 463.12 E-value: 2.00e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--G 81
Cdd:cd05970 50 FAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT----HHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 157
Cdd:cd05970 129 DNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 -SLG--LKAKMdagWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPI 234
Cdd:cd05970 209 yPLGhiVTAKY---WQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQ 314
Cdd:cd05970 286 IYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEID 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 315 IIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 394
Cdd:cd05970 366 LIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 395 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 474
Cdd:cd05970 446 GPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKT 523
|
490
....*....|....
gi 815659680 475 VTGKIQRAKLRDKE 488
Cdd:cd05970 524 ISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2-490 |
9.10e-117 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 351.03 E-value: 9.10e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 81
Cdd:COG0318 25 LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:COG0318 103 -------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR 237
Cdd:COG0318 128 NAAAIAAALGLTPGDVVLVALplfhVFGLTVGLLAPLL----AGAT--LVLLPRFDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 238 MLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKI--KPGYMGTAASCYDVQ 314
Cdd:COG0318 202 RLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRPLPGVEVR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 315 IIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 394
Cdd:COG0318 282 IVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 395 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPK 473
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR------PGAELDaEELRAFLRERLARYKVPRRVEFVDELPR 430
|
490
....*....|....*..
gi 815659680 474 TVTGKIQRAKLRDKEWK 490
Cdd:COG0318 431 TASGKIDRRALRERYAA 447
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
4-488 |
3.96e-112 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 338.77 E-value: 3.96e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDE 83
Cdd:cd05974 3 FAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 ViqevdTVASEcPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:cd05974 81 N-----THADD-PML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVGH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD 243
Cdd:cd05974 115 LSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 244 LSSYKFPhLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETglTCMVSKT--MKIKPGYMGTAASCYDVQIIDDKGN 321
Cdd:cd05974 195 LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET--TALVGNSpgQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 322 vlpPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN 401
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 402 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQR 481
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 815659680 482 AKLRDKE 488
Cdd:cd05974 426 VELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
4-488 |
7.24e-112 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 342.65 E-value: 7.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAK 76
Cdd:PRK04319 76 YKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIvgplfeaFMEEAVRD-------RLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIVAGDEVIQEVdtVASECPSLRIKLLVSE--KSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK---- 150
Cdd:PRK04319 148 VLITTPALLERK--PADDLPSLKHVLLVGEdvEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKgvlh 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 ----MAEHSYSSlglKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPI 226
Cdd:PRK04319 226 vhnaMLQHYQTG---KYVLD-----LHEDDVYWCTADPGWVTGTSYGIFAPWLNGA-TNVIDGGRFSPERWYRILEDYKV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 227 KSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSKT--MKIKP 301
Cdd:PRK04319 297 TVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETG-GIMIANYpaMDIKP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 302 GYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIrvKPIRPiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMG 381
Cdd:PRK04319 376 GSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQG 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 382 RANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYK 460
Cdd:PRK04319 453 RVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRP---GYEPsEELKEEIRGFVKKGLGAHA 529
|
490 500
....*....|....*....|....*...
gi 815659680 461 YPRKIEFVLNLPKTVTGKIQRAKLRDKE 488
Cdd:PRK04319 530 APREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2-486 |
1.24e-109 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 332.47 E-value: 1.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 81
Cdd:cd05971 7 VTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd05971 85 -------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGL--QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 239
Cdd:cd05971 116 HLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 240 LQQDLSSYKFP-HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGL---TCmvSKTMKIKPGYMGTAASCYDVQI 315
Cdd:cd05971 196 RQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvigNC--SALFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 316 IDDKGNVLPPGTEGDIGIRvkpiRPIGI-FSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 394
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 395 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 474
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
490
....*....|..
gi 815659680 475 VTGKIQRAKLRD 486
Cdd:cd05971 428 ATGKIRRRELRA 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
2-488 |
1.59e-102 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 314.44 E-value: 1.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTvasECPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd05969 80 EELYERTDP---EDPTL----------------------------------------LHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGaCTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 241
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG-VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 242 QD---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQII 316
Cdd:cd05969 196 EGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETG-SIMIANypCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 317 DDKGNVLPPGTEGDIGIrvKPIRPiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGP 396
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 397 SEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 475
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 815659680 476 TGKIQRAKLRDKE 488
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2-485 |
2.36e-98 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 304.49 E-value: 2.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEviqevdtvasecpslrikllvsekscdgwlnFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd05936 104 VS-------------------------------FTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTG--LQASDIMwtisdtgwiLNIL---------CSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMM 230
Cdd:cd05936 153 NALQIKAWLEdlLEGDDVV---------LAALplfhvfgltVALLLPLALGAT--IVLIPRFRPIGVLKEIRKHRVTIFP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAA 308
Cdd:cd05936 222 GVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRgDFWLL-GDRGIKDEDGYFQFMGRAND 385
Cdd:cd05936 302 PGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAFV-DGWLRtGDIGYMDEDGYFFIVDRKKD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 386 IINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLTK-ELQQHVKSVTAPYKYPRK 464
Cdd:cd05936 374 MIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGASLTEeEIIAFCREQLAGYKVPRQ 447
|
490 500
....*....|....*....|.
gi 815659680 465 IEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05936 448 VEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
4-485 |
5.51e-95 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 294.81 E-value: 5.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagde 83
Cdd:cd05973 3 FGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevdTVASECPSLRIKLLVsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-GLK 162
Cdd:cd05973 78 ------TDAANRHKLDSDPFV----------------------------------MMFTSGTTGLPKGVPVPLRALaAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AKMDAGwTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 242
Cdd:cd05973 118 AYLRDA-VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 243 DLSSYKFP--HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcMV-----SKTMKIKPGYMGTAASCYDVQI 315
Cdd:cd05973 196 GAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG---MVlanhhALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 316 IDDKGNVLPPGTEGDIGIRVKPiRPIGIFSGYVDNPDKTAAnirGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIG 395
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIAN-SPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 396 PSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 474
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG---GHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|.
gi 815659680 475 VTGKIQRAKLR 485
Cdd:cd05973 426 PSGKIQRFLLR 436
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
139-480 |
2.08e-90 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 279.56 E-value: 2.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACtfVHLLPKFDPLVIL 218
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFG-LLGALLAGGT--VVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSK 295
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 296 TMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 375
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlSHDPEqltkELQQHVKSV 455
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAE----ELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQ 480
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
6-485 |
1.45e-84 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 270.01 E-value: 1.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 6 ELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI 85
Cdd:cd05959 34 ELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 86 QEVDTVASECPSLRIKLLVS--EKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:cd05959 113 PVLAAALTKSEHTLVVLIVSggAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKF-DPLVILKTLSSYPIKSMMGAPIVYR-MLL 240
Cdd:cd05959 193 ELYARNVlGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTV--LMPERpTPAAVFKRIRRYRPTVFFGVPTLYAaMLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 241 QQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKG 320
Cdd:cd05959 271 APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 321 NVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVE 400
Cdd:cd05959 351 GDVADGEPGELYVRGPSSAT-----MYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 401 NALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQ 480
Cdd:cd05959 426 SALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQ 503
|
....*
gi 815659680 481 RAKLR 485
Cdd:cd05959 504 RFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2-490 |
1.87e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.44 E-value: 1.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK06187 32 TTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEKSCDG----WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 157
Cdd:PRK06187 111 SEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLGLKAKMDAGWTGLQASDI------MWTISDTGWilnilcSLMePWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMG 231
Cdd:PRK06187 191 NLFLHSLAVCAWLKLSRDDVylvivpMFHVHAWGL------PYL-ALMAGA-KQV-IPRRFDPENLLDLIETERVTFFFA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 232 APIVYRMLLQ------QDLSSYKFphlqncVTVGESLLPETL-ENWRAQTGLDIRESYGQTETG--LTCMV-SKTMKIKP 301
Cdd:PRK06187 262 VPTIWQMLLKaprayfVDFSSLRL------VIYGGAALPPALlREFKEKFGIDLVQGYGMTETSpvVSVLPpEDQLPGQW 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 302 GYM---GTAASCYDVQIIDDKGNVLPPGtEGDIG-IRVKpirpiG--IFSGYVDNPDKTAANIRGDfWLL-GDRGIKDED 374
Cdd:PRK06187 336 TKRrsaGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVR-----GpwLMQGYWNRPEATAETIDGG-WLHtGDVGYIDED 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 375 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVK 453
Cdd:PRK06187 409 GYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL------KPGATLDaKELRAFLR 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 815659680 454 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 490
Cdd:PRK06187 483 GRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2-485 |
1.65e-81 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 260.10 E-value: 1.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstdilyrlqmskakaivag 81
Cdd:cd05958 11 WTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI---------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdTVASEcPSLRIKllvsekscdgwlNFKKLLNEASTTHH-CVE--TGSQEASAIYFTSGTSGLPKMAEHSYSS 158
Cdd:cd05958 63 --------AVATM-PLLRPK------------ELAYILDKARITVAlCAHalTASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKmdaGWT----GLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMGAPI 234
Cdd:cd05958 122 PLASAD---RYAvnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV--LLEEATPDLLLSAIARYKPTVLFTAPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLL------QQDLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAA 308
Cdd:cd05958 197 AYRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpigifSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDII 387
Cdd:cd05958 272 PGYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSDDMI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 388 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflsHDP-EQLTKELQQHVKSVTAPYKYPRKIE 466
Cdd:cd05958 344 VSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---VIPgPVLARELQDHAKAHIAPYKYPRAIE 420
|
490
....*....|....*....
gi 815659680 467 FVLNLPKTVTGKIQRAKLR 485
Cdd:cd05958 421 FVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
4-487 |
3.70e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.98 E-value: 3.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK07656 33 YAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIqEVDTVASEC-PSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 158
Cdd:PRK07656 112 FL-GVDYSATTRlPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKMDAGWTGLQASDIMWTISDT----GWILNILCSLMEpwalGACTFVHllPKFDPLVILKTLSSYPIKSMMGAPI 234
Cdd:PRK07656 191 LLSNAADWAEYLGLTEGDRYLAANPFfhvfGYKAGVNAPLMR----GATILPL--PVFDPDEVFRLIETERITVLPGPPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE-TGLTCM--VSKTMKIKPGYMGTAAS 309
Cdd:PRK07656 265 MYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEaSGVTTFnrLDDDRKTVAGTIGTAIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 310 CYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDI 386
Cdd:PRK07656 345 GVENKIVNELGEEVPVGEVGELLVR-------GpnVMKGYYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 387 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKI 465
Cdd:PRK07656 418 FIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------AELTEEeLIAYCREHLAKYKVPRSI 491
|
490 500
....*....|....*....|..
gi 815659680 466 EFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PRK07656 492 EFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
4-485 |
9.77e-74 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 239.67 E-value: 9.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:cd05919 13 YGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPKMAEHSY-SSLGLK 162
Cdd:cd05919 92 DI--------------------------------------------------AYLLY-SSGTTGPPKGVMHAHrDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKfDPLVILKTLSSYPIKSMMGAPIVY-RMLLQ 241
Cdd:cd05919 121 DAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 242 QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGN 321
Cdd:cd05919 200 CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 322 VLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN 401
Cdd:cd05919 280 TIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 402 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
....
gi 815659680 482 AKLR 485
Cdd:cd05919 433 FKLR 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-485 |
1.94e-73 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 238.35 E-value: 1.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 81
Cdd:cd05934 4 WTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqeVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd05934 81 ------VDPAS----------------------------------------------ILYTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGLQASDIMWTISDTGWIlNILC-SLMEPWALGAcTFVhLLPKFDPLVILKTLSSY--PIKSMMGAPIvyRM 238
Cdd:cd05934 109 AGYYSARRFGLGEDDVYLTVLPLFHI-NAQAvSVLAALSVGA-TLV-LLPRFSASRFWSDVRRYgaTVTNYLGAML--SY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 239 LLQQDLSSYKFPHLQNCVTVGESLlPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 318
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 319 KGNVLPPGTEGDIGIRvkPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 398
Cdd:cd05934 263 DGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 399 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 477
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL------RPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
....*...
gi 815659680 478 KIQRAKLR 485
Cdd:cd05934 415 KVAKAQLR 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
4-486 |
6.31e-73 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 239.36 E-value: 6.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:TIGR02262 33 YGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLRIKLLVSEKScDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:TIGR02262 112 LLPVIKAALGKSPHLEHRVVVGRPE-AGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR-MLLQ 241
Cdd:TIGR02262 191 ELYARNTlGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA-TTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLAD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 242 QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGN 321
Cdd:TIGR02262 270 PNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 322 VLPPGTEGDIGIRvkpirpiGIFS--GYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEV 399
Cdd:TIGR02262 350 DVADGEPGELLIS-------GPSSatMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 400 ENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 479
Cdd:TIGR02262 423 ESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKI 497
|
....*..
gi 815659680 480 QRAKLRD 486
Cdd:TIGR02262 498 QRFKLRE 504
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
2-481 |
9.57e-72 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 234.43 E-value: 9.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 81
Cdd:cd17631 21 LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-- 159
Cdd:cd17631 98 DDLAL----------------------------------------------------LMYTSGTTGRPKGAMLTHRNLlw 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 -----GLKAKMDAGWTGLQASDIMWTISDTGWILNILcslmepwALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPI 234
Cdd:cd17631 126 navnaLAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL-------LRGGT--VVILRKFDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLLQQ-DLSSYKFPHLQnCVTVGESLLPE-TLENWRAqTGLDIRESYGQTETG-LTCMVSKTMKI-KPGYMGTAASC 310
Cdd:cd17631 197 MIQALLQHpRFATTDLSSLR-AVIYGGAPMPErLLRALQA-RGVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 311 YDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDfWLL-GDRGIKDEDGYFQFMGRANDIINS 389
Cdd:cd17631 275 VEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDG-WFHtGDLGRLDEDGYLYIVDRKKDMIIS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 390 SGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFV 468
Cdd:cd17631 349 GGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR------PGAELDeDELIAHCRERLARYKIPKSVEFV 422
|
490
....*....|...
gi 815659680 469 LNLPKTVTGKIQR 481
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2-486 |
5.90e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 226.74 E-value: 5.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 158
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGgreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 L---GLKAKMDAGWTglqASDIMwtisdtgwiLNIL----CSLME----PW-ALGACTfvHLLPKFDPLVILKTLSSYPI 226
Cdd:PRK08316 196 LiaeYVSCIVAGDMS---ADDIP---------LHALplyhCAQLDvflgPYlYVGATN--VILDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 227 KSMMGAPIVYRMLL------QQDLSSykfphLQNCVtVGESLLP-ETLENWRAQ-TGLDIRESYGQTETGLTCMV--SKT 296
Cdd:PRK08316 262 TSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGY-YGASIMPvEVLKELRERlPGLRFYNCYGQTEIAPLATVlgPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 297 MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGY 376
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SP----QLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 377 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSV 455
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDELIAHCRAR 484
|
490 500 510
....*....|....*....|....*....|.
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK08316 485 LAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
4-492 |
1.07e-67 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 228.35 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FmpgtiqmKSTDILYRLQMSKAK 76
Cdd:cd05967 85 YAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsvvfggF-------AAKELASRIDDAKPK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIVA------GDEVIQE---VDTVASECPSLRIKLLV---SEKSCD-----GWLNFKKLLNEAsTTHHCVETGSQEASAI 139
Cdd:cd05967 157 LIVTascgiePGKVVPYkplLDKALELSGHKPHHVLVlnrPQVPADltkpgRDLDWSELLAKA-EPVDCVPVAATDPLYI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 140 YFTSGTSGLPK-----MAEHSyssLGLKAKMDAGWtGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVH-----LL 209
Cdd:cd05967 236 LYTSGTTGKPKgvvrdNGGHA---VALNWSMRNIY-GIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYegkpvGT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 210 PkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD-----LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQ 284
Cdd:cd05967 312 P--DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 285 TETG----LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVDNPDKTAANIRG 360
Cdd:cd05967 390 TETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPP-GCLLTLWKNDERFKKLYLS 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 361 DF---WLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfL 437
Cdd:cd05967 468 KFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-V 546
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 815659680 438 SHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD----KEWKMS 492
Cdd:cd05967 547 KITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKiadgEDYTIP 605
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
4-486 |
6.15e-67 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 221.78 E-value: 6.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGde 83
Cdd:cd05941 14 YADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLDP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLG--L 161
Cdd:cd05941 92 -----------------------------------------------------ALILYTSGTTGRPKGVVLTHANLAanV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAgWTglqasdimWTISDT-----------GWILNILCSLmepWALGACtfvHLLPKFDPLVILKTLSSYPIKSMM 230
Cdd:cd05941 119 RALVDA-WR--------WTEDDVllhvlplhhvhGLVNALLCPL---FAGASV---EFLPKFDPKEVAISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRMLLQQdlSSYKFPHLQNCVTVGES-----------LLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKI 299
Cdd:cd05941 184 GVPTIYTRLLQY--YEAHFTDPQFARAAAAErlrlmvsgsaaLPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 300 KPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYF 377
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRAN-DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEqltkELQQHVKSVT 456
Cdd:cd05941 337 WILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQRL 412
|
490 500 510
....*....|....*....|....*....|
gi 815659680 457 APYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
2-486 |
1.59e-65 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 219.49 E-value: 1.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA---IYFTSGTSGLPKMAEHSYSS 158
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlalILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRM 238
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS--VVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 239 LLQQDLSSY--KFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSKTMKIKPGYMGTAASCyDVQ 314
Cdd:cd05926 252 LLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 315 IIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSSGYR 393
Cdd:cd05926 331 ILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 394 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 473
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE-----GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPK 480
|
490
....*....|...
gi 815659680 474 TVTGKIQRAKLRD 486
Cdd:cd05926 481 TATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2-480 |
8.60e-65 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 217.47 E-value: 8.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRiKLLVSEKSCDGWLNFKKLLNEASTTHH-----CVETGSQEASAIYFTSGTSGLPKMAEHSY 156
Cdd:cd05911 90 PDGLEKVKEAAKELGPKD-KIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLglkakmdagwtgLQASDIMWTISDTGWILN--ILCSLMEPWALGACTFVHLL---------PKFDPLVILKTLSSYP 225
Cdd:cd05911 169 RNL------------IANLSQVQTFLYGNDGSNdvILGFLPLYHIYGLFTTLASLlngatviimPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 226 IKSMMGAP-IVYRMLLQQDLSSYKFPHLQNcVTVG--------ESLLPETLENWRaqtgldIRESYGQTETGLTCMVSKT 296
Cdd:cd05911 237 ITFLYLVPpIAAALAKSPLLDKYDLSSLRV-ILSGgaplskelQELLAKRFPNAT------IKQGYGMTETGGILTVNPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 297 MKIKPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDED 374
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 375 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVK 453
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK------PGEKLTeKEVKDYVA 458
|
490 500
....*....|....*....|....*...
gi 815659680 454 SVTAPYKYPRK-IEFVLNLPKTVTGKIQ 480
Cdd:cd05911 459 KKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2-486 |
1.18e-64 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 220.13 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEwwLVI--LGCIRAGLI-------FMPGTIQMkstdilyRLQM 72
Cdd:cd05966 85 ITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPE--LVIamLACARIGAVhsvvfagFSAESLAD-------RIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 73 SKAKAIVAGDE------VI---QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQ 134
Cdd:cd05966 155 AQCKLVITADGgyrggkVIplkEIVDEALEKCPSVE-KVLVVKRTGgevpmtegrDLWWH--DLMAKQSPECEPEWMDSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 135 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkfd 213
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVfDYHPDDIYWCTADIGWITGHSYIVYGPLANGATT--------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 214 plVILKTLSSYPIKSMM-------------GAPIVYRMLLQQ--------DLSSYKFPHlqncvTVGESLLPETLENWRA 272
Cdd:cd05966 303 --VMFEGTPTYPDPGRYwdivekhkvtifyTAPTAIRALMKFgdewvkkhDLSSLRVLG-----SVGEPINPEAWMWYYE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 273 QTG---LDIRESYGQTETG---LTCMVSKTmKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPI-GIFS 345
Cdd:cd05966 376 VIGkerCPIVDTWWQTETGgimITPLPGAT-PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK----RPWpGMAR 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 346 GYVDNPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 422
Cdd:cd05966 451 TIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 423 GEVVKAFVVLASqflSHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05966 531 GEAIYAFVTLKD---GEEPSDeLRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2-390 |
2.54e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.48 E-value: 2.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:pfam00501 22 LTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DE-VIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEAS----AIYFTSGTSGLPKMAEHS- 155
Cdd:pfam00501 101 DAlKLEELLEALGKLEVVKLVLVLDR---DPVLKEEPLPEEAKPADVPPPPPPPPDPddlaYIIYTSGTTGKPKGVMLTh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 ---YSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtfVHLLPKF---DPLVILKTLSSYP 225
Cdd:pfam00501 178 rnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLL----AGAT--VVLPPGFpalDPAALLELIERYK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 226 IKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIK---P 301
Cdd:pfam00501 252 VTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 302 GYMGTAASCYDVQIIDDK-GNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQF 379
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAFDEDGWYRtGDLGRRDEDGYLEI 406
|
410
....*....|.
gi 815659680 380 MGRANDIINSS 390
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
3-484 |
9.43e-64 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 213.11 E-value: 9.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGd 82
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 eviQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSSLGLK 162
Cdd:cd05935 81 ---SELDDLA---------------------------------------------LIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL-- 240
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG-TYV-LMARWDRETALELIEKYKVTFWTNIPTMLVDLLat 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 241 ----QQDLSSYKFphlqncVTVGESLLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQI 315
Cdd:cd05935 191 pefkTRDLSSLKV------LTGGGAPMPPAVaEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 316 ID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAA---NIRG-DFWLLGDRGIKDEDGYFQFMGRANDIINSS 390
Cdd:cd05935 265 IDiETGRELPPNEVGEIVVR-GP----QIFKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 391 GYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLN 470
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 815659680 471 LPKTVTGKIQRAKL 484
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
4-494 |
2.50e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 215.21 E-value: 2.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK08314 38 YRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEV------------------DTVASECP-----SLRIKLLVSEKSCDGWLnfkkLLNEASTTHHC---VETGSQEAS 137
Cdd:PRK08314 118 LAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPGGVV----AWKEALAAGLApppHTAGPDDLA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVI 217
Cdd:PRK08314 194 VLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGA-TVV-LMPRWDREAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 218 LKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQnCVTVGESLLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSK 295
Cdd:PRK08314 272 ARLIERYRVTHWTNIPtMVVDFLASPGLAERDLSSLR-YIGGGGAAMPEAVaERLKELTGLDYVEGYGLTETMAQTHSNP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 296 TMKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAA---NIRGD-FWLLGDR 368
Cdd:PRK08314 351 PDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-------GpqVFKGYWNRPEATAEafiEIDGKrFFRTGDL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 369 GIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQltkEL 448
Cdd:PRK08314 424 GRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EI 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 815659680 449 QQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGK 494
Cdd:PRK08314 501 IAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-479 |
3.49e-63 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 215.90 E-value: 3.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd17634 85 ISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTV----------ASECPSLRIKLLVSEKSCD------GWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGT 145
Cdd:cd17634 164 DGGVRAGRSVplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 146 SGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHL-LPKF-DPLVILKTLS 222
Cdd:cd17634 244 TGKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 SYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETLE-NWR--AQTGLDIRESYGQTETGLTCMvskt 296
Cdd:cd17634 324 KHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGGFMI---- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 297 mKIKPGYMGTAASC-------YDVQIIDDKGNVLPPGTEGDIGIRVKpiRPIGIFSGYVDNPDKTAANIR--GDFWLLGD 367
Cdd:cd17634 400 -TPLPGAIELKAGSatrpvfgVQPAVVDNEGHPQPGGTEGNLVITDP--WPGQTRTLFGDHERFEQTYFStfKGMYFSGD 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 368 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKE 447
Cdd:cd17634 477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAE 554
|
490 500 510
....*....|....*....|....*....|..
gi 815659680 448 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 479
Cdd:cd17634 555 LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2-487 |
9.91e-60 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 204.72 E-value: 9.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSekscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETLDA----DGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKM--DA-GWTG----LQASDIMWTisdTGWILNILCSLMEpwalGACTFvhLLPKFDPLVILKTLSSypIKSMMGAPI 234
Cdd:PRK07514 184 NALTlvDYwRFTPddvlIHALPIFHT---HGLFVATNVALLA----GASMI--FLPKFDPDAVLALMPR--ATVMMGVPT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcmvsktMKI--------KPGYMG 305
Cdd:PRK07514 253 FYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN--------MNTsnpydgerRAGTVG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 306 TAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMG 381
Cdd:PRK07514 325 FPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 382 RANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfVVLASQFLSHDPEQLTKELQQHVksvtAPYKY 461
Cdd:PRK07514 398 RGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGAALDEAAILAALKGRL----ARFKQ 472
|
490 500
....*....|....*....|....*.
gi 815659680 462 PRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PRK07514 473 PKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4-484 |
1.71e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 205.27 E-value: 1.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK06178 61 YAELDELSDRFAALLRQR-GVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASEC-----------------PSLRIKLLVSE--KSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSG 144
Cdd:PRK06178 140 LAPVVEQVRAETslrhvivtsladvlpaePTLPLPDSLRAprLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 145 TSGLPKMAEHSYSSLGLKAKMDAGWTG-LQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSS 223
Cdd:PRK06178 220 TTGMPKGCEHTQRDMVYTAAAAYAVAVvGGEDSVFLSFLPEFWIAGENFGLLFPLFSGA-TLV-LLARWDAVAFMAAVER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 224 YPIKSMMGAPIVYRMLL------QQDLSSYKFPhlqNCVTVGESLLPETLENWRAQTGLDIRE-SYGQTETGlTC----- 291
Cdd:PRK06178 298 YRVTRTVMLVDNAVELMdhprfaEYDLSSLRQV---RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETH-TCdtfta 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 292 -MVSKTMKIK--PGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRgDFWL-LG 366
Cdd:PRK06178 374 gFQDDDFDLLsqPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVR-TP----SLLKGYWNKPEATAEALR-DGWLhTG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 367 DRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTK 446
Cdd:PRK06178 448 DIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAA 522
|
490 500 510
....*....|....*....|....*....|....*...
gi 815659680 447 ELQQHVKSVTAPYKYPrKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK06178 523 ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-490 |
4.26e-59 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.83 E-value: 4.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQ-----EVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 155
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 YSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMGA-PI 234
Cdd:PRK06087 209 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLALLEQQRCTCMLGAtPF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRML--LQQ---DLSSYKFphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMV--SKTMKIKPGYMGTA 307
Cdd:PRK06087 287 IYDLLnlLEKqpaDLSALRF------FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVnlDDPLSRFMHTDGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDKGNVLPPGTEGDigirvKPIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDI 386
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 387 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKEL-QQHVksvtAPYKYPRKI 465
Cdd:PRK06087 436 IVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRV----AKYKYPEHI 511
|
490 500
....*....|....*....|....*
gi 815659680 466 EFVLNLPKTVTGKIQRAKLRdKEWK 490
Cdd:PRK06087 512 VVIDKLPRTASGKIQKFLLR-KDIM 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
2-495 |
2.02e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 200.90 E-value: 2.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK08276 12 VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPK----------- 150
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET---AGADMLYSSGTTGRPKgikrplpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 --MAEHSYSSLGLKAKMDAGWTGLQASDIMWTiSDTGWILNILcslmepwALGAcTFVhLLPKFDPLVILKTLSSYPIKS 228
Cdd:PRK08276 168 deAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLRFGMSAL-------ALGG-TVV-VMEKFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 229 MMGAPIVY-RML-LQQ------DLSSYKF------PhlqnC-VTVGESLLpetlENWraqtGLDIRESYGQTET-GLTCM 292
Cdd:PRK08276 238 SQLVPTMFvRMLkLPEevraryDVSSLRVaihaaaP----CpVEVKRAMI----DWW----GPIIHEYYASSEGgGVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 293 VSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAANIRGDFWL-LGDRGIK 371
Cdd:PRK08276 306 TSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFE-YHNDPEKTAAARNPHGWVtVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 372 DEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQ 450
Cdd:PRK08276 380 DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD---GADAgDALAAELIA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 815659680 451 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 495
Cdd:PRK08276 457 WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
3-486 |
2.28e-57 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 197.91 E-value: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgD 82
Cdd:cd12118 31 TWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDTVASECPSLriKLLVSEKSCDgwlnfkkllneastthhcvetgsqeASAIYFTSGTSGLPKMAEHSYSSLGLK 162
Cdd:cd12118 109 REFEYEDLLAEGDPDF--EWIPPADEWD-------------------------PIALNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKSMMGAPIVYR 237
Cdd:cd12118 162 ALANILEWEMKQHPVyLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 238 MLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLTCMVSKT-----------MKIKPG 302
Cdd:cd12118 234 MLANaPPSDARPLPHRVH-VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETygpATVCAWKPEwdelpteerarLKARQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 303 --YMGTAAscydVQIIDDKGNVLPPG---TEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 375
Cdd:cd12118 313 vrYVGLEE----VDVLDPETMKPVPRdgkTIGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKS 454
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAKVTeEEIIAFCRE 455
|
490 500 510
....*....|....*....|....*....|..
gi 815659680 455 VTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRD 486
Cdd:cd12118 456 HLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
4-485 |
7.40e-57 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.21 E-value: 7.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK08008 40 YLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 ---VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT-HHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL 159
Cdd:PRK08008 119 fypMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATlCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 239
Cdd:PRK08008 199 RFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA-TFV-LLEKYSARAFWGQVCKYRATITECIPMMIRTL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 240 LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETgLTCMVSKTmkikPG------YMGTAASCYDV 313
Cdd:PRK08008 277 MVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYGMTET-IVGIIGDR----PGdkrrwpSIGRPGFCYEA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 314 QIIDDKGNVLPPGTEGDIGIRVKPIRPIgiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGY 392
Cdd:PRK08008 352 EIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 393 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNL 471
Cdd:PRK08008 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN------EGETLSEEeFFAFCEQNMAKFKVPSYLEIRKDL 503
|
490
....*....|....
gi 815659680 472 PKTVTGKIQRAKLR 485
Cdd:PRK08008 504 PRNCSGKIIKKNLK 517
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
4-486 |
1.17e-56 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 199.21 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAK 76
Cdd:PRK00174 101 YRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggFSAEALAD-------RIIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIVAGDEVI---------QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQEASA 138
Cdd:PRK00174 173 LVITADEGVrggkpiplkANVDEALANCPSVE-KVIVVRRTGgdvdwvegrDLWWH--ELVAGASDECEPEPMDAEDPLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkf 212
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD-----YKDGDVYWCTADVGWVTGHSYIVYGPLANGATT-------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 dplVILKTLSSYPIKSMMG-------------APIVYRMLLQQ--------DLSSYKFPHlqncvTVGESLLPETLENWR 271
Cdd:PRK00174 317 ---LMFEGVPNYPDPGRFWevidkhkvtifytAPTAIRALMKEgdehpkkyDLSSLRLLG-----SVGEPINPEAWEWYY 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 272 AQTGLD---IRESYGQTETGlTCMVSK---TMKIKPGymgtaaSC------YDVQIIDDKGNVLPPGTEGDIGIRvKP-- 337
Cdd:PRK00174 389 KVVGGErcpIVDTWWQTETG-GIMITPlpgATPLKPG------SAtrplpgIQPAVVDEEGNPLEGGEGGNLVIK-DPwp 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 338 --IRPIgifsgYVDnPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVET 412
Cdd:PRK00174 461 gmMRTI-----YGD-HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA 534
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 413 AVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK00174 535 AVVGRPDDIKGQGIYAFVTLKG---GEEPsDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2-485 |
1.79e-56 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 198.10 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05968 92 LTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 D---------EVIQEVDTVASECPSLRiKLLVSE--KSCDGWLNFKKL---LNEASTTHHCVETGSQEASAIYFTSGTSG 147
Cdd:cd05968 171 DgftrrgrevNLKEEADKACAQCPTVE-KVVVVRhlGNDFTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 148 LPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWilnilcsLMEPWA------LGACTFVHL-LPKFD-PLVIL 218
Cdd:cd05968 250 KPKGTVHVHAGFPLKAAQDMYFQfDLKPGDLLTWFTDLGW-------MMGPWLifggliLGATMVLYDgAPDHPkADRLW 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIKSMMGAPIVYRMLL--------QQDLSSykfphLQNCVTVGESLLPETLeNWRAQTGLD----IRESYGQTE 286
Cdd:cd05968 323 RMVEDHEITHLGLSPTLIRALKprgdapvnAHDLSS-----LRVLGSTGEPWNPEPW-NWLFETVGKgrnpIINYSGGTE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 287 TG---LTCMVSKtmKIKPGYMGTAASCYDVQIIDDKGNVLPPgTEGDIGIRvKPIrpIGIFSGYVDNPDK---TAANIRG 360
Cdd:cd05968 397 ISggiLGNVLIK--PIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-APW--PGMTRGFWRDEDRyleTYWSRFD 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 361 DFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHD 440
Cdd:cd05968 471 NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TP 548
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 815659680 441 PEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05968 549 TEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2-485 |
1.15e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 196.33 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGlIFMPGTIQMKSTDILYRLQMSKAKAIVA- 80
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 ----GDEVIQEVDTVASECPSLR-----------------IKLLVSEKSCDGWLNFKKLLNEASTTHHCVET--GSQEAS 137
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRpiGPDDVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYFTSGTSGLPKMAEHSYSSLglkakMDAGWTGLQASDImwTISDTgwilnILCSL------------MEPWALGAcTF 205
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGNE-----VANAWLGALLLGL--GPGDT-----VFCGLplfhvnallvtgLAPLARGA-HV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 206 VHLLPK--FDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-----DLSSYKFphlqncVTVGESLLP-ETLENWRAQT 274
Cdd:PRK07529 284 VLATPQgyRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY------ALCGAAPLPvEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 275 GLDIRESYGQTETglTCMVS---KTMKIKPGYMGTAASCYDVQII--DDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVd 349
Cdd:PRK07529 358 GVRIVEGYGLTEA--TCVSSvnpPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLC--IAGPNVFSGYL- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 350 NPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKA 428
Cdd:PRK07529 433 EAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 815659680 429 FVVLA--SQFlshDPEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK07529 513 YVQLKpgASA---TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2-486 |
1.41e-54 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 191.51 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLVSEKSCDGW-LNFKKL-LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL 159
Cdd:PRK06155 126 AALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWTGLQASDIMWT---ISDTGwILNILCSLMepwaLGACTFVhLLPKF------DPLVILKTLSSYPIKSMM 230
Cdd:PRK06155 206 YWWGRNSAEDLEIGADDVLYTtlpLFHTN-ALNAFFQAL----LAGATYV-LEPRFsasgfwPAVRRHGATVTYLLGAMV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 gapivyRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKiKPGYMGTAASC 310
Cdd:PRK06155 280 ------SILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 311 YDVQIIDDKGNVLPPGTEGDIGIRVKPirPIGIFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINS 389
Cdd:PRK06155 352 FEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKDAIRR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 390 SGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLaSQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVL 469
Cdd:PRK06155 429 RGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTALEPV----ALVRHCEPRLAYFAVPRYVEFVA 503
|
490
....*....|....*..
gi 815659680 470 NLPKTVTGKIQRAKLRD 486
Cdd:PRK06155 504 ALPKTENGKVQKFVLRE 520
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
4-485 |
3.59e-54 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 187.97 E-value: 3.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:cd05903 4 YSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevdtvasecpslrikllvsekscdgwlnFKKllneasttHHCVETGSQEAsAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:cd05903 83 -------------------------------FRQ--------FDPAAMPDAVA-LLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGA-PIVYRMLLQQ 242
Cdd:cd05903 123 RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 243 DLSSYKFPHLQnCVTVGESLLPETLENwRAQT--GLDIRESYGQTETGltcmvSKTMKIKPGYMGtAASCYD-------- 312
Cdd:cd05903 201 EEAGEPLSRLR-TFVCGGATVPRSLAR-RAAEllGAKVCSAYGSTECP-----GAVTSITPAPED-RRLYTDgrplpgve 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 313 VQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGY 392
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 393 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLN 470
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPERLVHVDD 421
|
490
....*....|....*
gi 815659680 471 LPKTVTGKIQRAKLR 485
Cdd:cd05903 422 LPRTPSGKVQKFRLR 436
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-490 |
3.79e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 188.32 E-value: 3.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK06710 52 FSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASecpSLRIKLLVSEKSCDgWLNFKKLL----------------NEASTTH--HCVE----TG-------SQ 134
Cdd:PRK06710 131 VFPRVTNVQS---ATKIEHVIVTRIAD-FLPFPKNLlypfvqkkqsnlvvkvSESETIHlwNSVEkevnTGvevpcdpEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 135 EASAIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdIMWTISDTGWILNilCSLMEPWALGACTFVH------- 207
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNL-----------------VSNTLMGVQWLYN--CKEGEEVVLGVLPFFHvygmtav 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 208 ------------LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQT 274
Cdd:PRK06710 268 mnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 275 GLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPD 352
Cdd:PRK06710 348 GGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYWNKPE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 353 KTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 431
Cdd:PRK06710 423 ETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 815659680 432 lasqfLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 490
Cdd:PRK06710 502 -----LKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
3-486 |
1.23e-52 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 185.91 E-value: 1.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 79
Cdd:cd12119 27 TYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVASECPSLRIKLLVS------EKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 153
Cdd:cd12119 103 VDRDFLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 154 HSYSSLGLKA--KMDAGWTGLQASDIMWTISD----TGWILNILCSLmepwaLGACtfvHLLP--KFDPLVILKTLSSYP 225
Cdd:cd12119 183 YSHRSLVLHAmaALLTDGLGLSESDVVLPVVPmfhvNAWGLPYAAAM-----VGAK---LVLPgpYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 226 IKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK--------- 295
Cdd:cd12119 255 VTFAAGVPTVWQGLLDhLEANGRDLSSLRR-VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARppsehsnls 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 296 -----TMKIKPGYmgtaaSCYDVQ--IIDDKGNVLP--PGTEGDIGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWLLG 366
Cdd:cd12119 334 edeqlALRAKQGR-----PVPGVElrIVDDDGRELPwdGKAVGELQVR-GPW----VTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 367 DRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT- 445
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK------EGATVTa 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 815659680 446 KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2-497 |
8.10e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 183.65 E-value: 8.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVI-----LGCIRAGLIFMpGTIQmkstDILYRLQMSKAK 76
Cdd:PRK06188 38 LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIgaaqlAGLRRTALHPL-GSLD----DHAYVLEDAGIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIVAGDEVIQE-VDTVASECPSLRIKLLVSEksCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 155
Cdd:PRK06188 112 TLIVDPAPFVErALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 YSSLglkakmdAGWTGLQASDIMWT----------ISDTGWILnILCSLMEpwalGActFVHLLPKFDPLVILKTLSSYP 225
Cdd:PRK06188 190 HRSI-------ATMAQIQLAEWEWPadprflmctpLSHAGGAF-FLPTLLR----GG--TVIVLAKFDPAEVLRAIEEQR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 226 IKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPEtlenwRAQTGLDI-----RESYGQTETGLTCMVSKTMKI 299
Cdd:PRK06188 256 ITATFLVPtMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpifAQYYGQTEAPMVITYLRKRDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 300 KPGYMGTAASC------YDVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNPDKTAANIRGDfWL-LGDRGIKD 372
Cdd:PRK06188 331 DPDDPKRLTSCgrptpgLRVALLDEDGREVAQGEVGEICVR-GPL----VMDGYWNRPEETAEAFRDG-WLhTGDVARED 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 373 EDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHV 452
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVDAA----ELQAHV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 815659680 453 KSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWkmSGKARA 497
Cdd:PRK06188 480 KERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW--EGRGRA 522
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-486 |
1.73e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 183.82 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 D--------EVIQEV--DTVASEC--------PSLRIKLLVSEKSCDGWLNFKKLLNEAST-THHCVETGSQ-----EAS 137
Cdd:PRK12583 125 DafktsdyhAMLQELlpGLAEGQPgalacerlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQAsldrdDPI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWIL-NILCSlmepwALGACTfvhLLPK- 211
Cdd:PRK12583 205 NIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhcfGMVLaNLGCM-----TVGACL---VYPNe 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 212 -FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQTETG 288
Cdd:PRK12583 277 aFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 289 ----LTCmVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL 364
Cdd:PRK12583 357 pvslQTT-AADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR-----GYSVMKGYWNNPEATAESIDEDGWM 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 365 -LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQ 443
Cdd:PRK12583 431 hTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRL------HPGHA 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 815659680 444 LT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK12583 505 ASeEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
4-486 |
1.57e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 180.99 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgtiqmkSTDILY-------RLQMSKAK 76
Cdd:PRK07059 51 YGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-------NVNPLYtprelehQLKDSGAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIV-------AGDEVIQEVDT----VASECPSL------------RIKLLVSEKSCDGWLNFKKLLNE-ASTTHHCVETG 132
Cdd:PRK07059 123 AIVvlenfatTVQQVLAKTAVkhvvVASMGDLLgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEgARQTFKPVKLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 133 SQEASAIYFTSGTSGLPKMAEHSYSS-LGLKAKMDAgWtgLQASDIMWTISDTgwiLNILCSLmeP----WALGACTFVH 207
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMEA-W--LQPAFEKKPRPDQ---LNFVCAL--PlyhiFALTVCGLLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 208 --------LLPkfDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTG 275
Cdd:PRK07059 275 mrtggrniLIP--NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 276 LDIRESYGQTETG--LTCMVSKTMKIKpGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNP 351
Cdd:PRK07059 353 CPITEGYGLSETSpvATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-------GpqVMAGYWNRP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 352 DKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFV 430
Cdd:PRK07059 425 DETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 815659680 431 VlasqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK07059 505 V------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2-484 |
4.66e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 178.52 E-value: 4.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DE---VIQEVDTVASECPSLRIKLL--VSEKSCDGWlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPKMAEHSY 156
Cdd:PRK06839 108 KTfqnMALSMQKVSYVQRVISITSLkeIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHllPKFDPLVILKTLSSYPIKSMMGAPIVY 236
Cdd:PRK06839 172 ENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMGVPTIH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 237 RMLLQQ-DLSSYKFPHLQNCVTvGESLLPETLENWRAQTGLDIRESYGQTETGLTC-MVSKT-MKIKPGYMGTAASCYDV 313
Cdd:PRK06839 250 QALINCsKFETTNLQSVRWFYN-GGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfMLSEEdARRKVGSIGKPVLFCDY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 314 QIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYR 393
Cdd:PRK06839 329 ELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGEN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 394 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltKELQQHVKSVTAPYKYPRKIEFVLNLPK 473
Cdd:PRK06839 404 IYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFLKELPK 478
|
490
....*....|.
gi 815659680 474 TVTGKIQRAKL 484
Cdd:PRK06839 479 NATGKIQKAQL 489
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
4-487 |
8.62e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 178.82 E-value: 8.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK07786 45 WRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:PRK07786 124 LAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDA-GWTGLQASDI------MWTISDTGwilNILCSLMepwaLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY 236
Cdd:PRK07786 204 MTCLrTNGADINSDVgfvgvpLFHIAGIG---SMLPGLL----LGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 237 RMLL------QQDLSsykfphLQNcVTVGESLLPETLENWRAQT--GLDIRESYGQTE-TGLTCMVSKTMKI-KPGYMGT 306
Cdd:PRK07786 277 QAVCaeqqarPRDLA------LRV-LSWGAAPASDTLLRQMAATfpEAQILAAFGQTEmSPVTCMLLGEDAIrKLGSVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 307 AASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDI 386
Cdd:PRK07786 350 VIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDM 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 387 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLT-KELQQHVKSVTAPYKYPRKI 465
Cdd:PRK07786 425 IISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN-----DDAALTlEDLAEFLTDRLARYKHPKAL 499
|
490 500
....*....|....*....|..
gi 815659680 466 EFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PRK07786 500 EIVDALPRNPAGKVLKTELRER 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
23-485 |
1.08e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 176.48 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 23 GLQRGDRVAVVLPRVPEWWLVILGCIRAG----LIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSL 98
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 99 RIKLLVsekscDGWLNfkkllNEASTTHHCVEtgSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM 178
Cdd:cd05922 94 GTVLDA-----DGIRA-----ARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 179 WTISDTGWI--LNILCSLMEpwaLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCV 256
Cdd:cd05922 162 LTVLPLSYDygLSVLNTHLL---RGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 257 TVGESLLPETLENWR-AQTGLDIRESYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGI 333
Cdd:cd05922 238 QAGGRLPQETIARLReLLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 334 RvkpiRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETA 413
Cdd:cd05922 318 R----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815659680 414 VISSPDPVrGEVVKAFVVLasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05922 394 AVGLPDPL-GEKLALFVTA-------PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
4-494 |
3.54e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 177.26 E-value: 3.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 80
Cdd:PRK05677 52 YGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVClan 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 ----GDEVIQE-------VDTVASECPSLR----------IKLLVSEKSCDGWLNFKKLLNE-ASTTHHCVETGSQEASA 138
Cdd:PRK05677 132 mahlAEKVLPKtgvkhviVTEVADMLPPLKrllinavvkhVKKMVPAYHLPQAVKFNDALAKgAGQPVTEANPQADDVAV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPK--MAEHSysslGLKAKMdagwtgLQASDIMwtisdtGWILNILCS-LMEPWALG-------ACTFVHL 208
Cdd:PRK05677 212 LQYTGGTTGVAKgaMLTHR----NLVANM------LQCRALM------GSNLNEGCEiLIAPLPLYhiyaftfHCMAMML 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 209 LPKFDPLV--------ILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIR 279
Cdd:PRK05677 276 IGNHNILIsnprdlpaMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAIC 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 280 ESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIR 359
Cdd:PRK05677 356 EGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GP----QVMKGYWQRPEATDEILD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 360 GDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfls 438
Cdd:PRK05677 431 SDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG--- 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 815659680 439 hdpEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGK 494
Cdd:PRK05677 508 ---ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGL 561
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2-484 |
3.55e-49 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 174.64 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivag 81
Cdd:cd05930 13 LTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqeVDTvasECPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTSGLPK--MAEH-SYSS 158
Cdd:cd05930 67 ------LDP---SYPAERLAYILED-----------------SGAKLVLTDPDDLAYVIYTSGSTGKPKgvMVEHrGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LgLKAKMDAgwTGLQASDIMWTISDTGWILnilcSLME---PWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGA 232
Cdd:cd05930 121 L-LLWMQEA--YPLTPGDRVLQFTSFSFDV----SVWEifgALLAGAT--LVVLPEevrKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 233 PIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTET--GLTCMVSKTMKIKPGYM--GTA 307
Cdd:cd05930 192 PSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtvDATYYRVPPDDEEDGRVpiGRP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAANIRGDFWLL-------GDRGIKDEDGYF 377
Cdd:cd05930 271 IPNTRVYVLDENLRPVPPGVPGELyigGA--------GLARGYLNRPELTAERFVPNPFGPgermyrtGDLVRWLPDGNL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHDPEQLTKELQQHVKSVTA 457
Cdd:cd05930 343 EFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD-----EGGELDEEELRAHLAERLP 417
|
490 500
....*....|....*....|....*..
gi 815659680 458 PYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
3-485 |
1.42e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.43 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDTVASECPsLRIKLlvsEKSCDGWLNFKKLLNEAS---TTHHCvetgsqeASAIYFTSGTSGLPKMAEHSYSSL 159
Cdd:PRK13390 105 ALDGLAAKVGADLP-LRLSF---GGEIDGFGSFEAALAGAGprlTEQPC-------GAVMLYSSGTTGFPKGIQPDLPGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMD------AGWTGLQASDIMWT------ISDTGWilnilCSLMEpwALGACtfVHLLPKFDPLVILKTLSSYPIK 227
Cdd:PRK13390 174 DVDAPGDpivaiaRAFYDISESDIYYSsapiyhAAPLRW-----CSMVH--ALGGT--VVLAKRFDAQATLGHVERYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 228 SMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESL---LPETLENWraqTGLDIRESYGQTET-GLTCMVSKTMKIK 300
Cdd:PRK13390 245 VTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWLAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 301 PGYMGTAAsCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAA--NIRGDFWL-LGDRGIKDEDGYF 377
Cdd:PRK13390 322 PGSVGRSV-LGDLHICDDDGNELPAGRIGTVYFE----RDRLPFR-YLNDPEKTAAaqHPAHPFWTtVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKSVT 456
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RGsDELARELIDYTRSRI 472
|
490 500
....*....|....*....|....*....
gi 815659680 457 APYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK13390 473 AHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
4-484 |
4.47e-48 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 173.19 E-value: 4.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 83
Cdd:cd05904 35 YAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqeVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MAEHSysslG 160
Cdd:cd05904 111 ----TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQdDVAALLYSSGTTGRSKgvMLTHR----N 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 LKAkMDAGWTGLQASDI-----------MWTISDTGWILniLCSLmepwALGACTFVhlLPKFDPLVILKTLSSYPIKSM 229
Cdd:cd05904 183 LIA-MVAQFVAGEGSNSdsedvflcvlpMFHIYGLSSFA--LGLL----RLGATVVV--MPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 230 MGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETG---LTCMVSKTMKIKPGYM 304
Cdd:cd05904 254 PVVPpIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTgvvAMCFAPEKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 382
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 383 ANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQ-FLSHDpeqltkELQQHVKSVTAPYKY 461
Cdd:cd05904 409 LKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGsSLTED------EIMDFVAKQVAPYKK 482
|
490 500
....*....|....*....|...
gi 815659680 462 PRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05904 483 VRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
188-481 |
1.29e-47 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 167.83 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 188 LNILCSLMEpwaLGACTFVhlLPKFDPLVILKTLSSYPIkSMMG--APIVYRMLLQQDLSSYKFPHLQNcvtVGESLLPE 265
Cdd:cd17637 56 LNLALATFH---AGGANVV--MEKFDPAEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSLRH---VLGLDAPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 266 TLENWRAQTGLDIRESYGQTET-GLTCMVSKTMKikPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIF 344
Cdd:cd17637 127 TIQRFEETTGATFWSLYGQTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 345 SGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGR--ANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 422
Cdd:cd17637 200 QGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKW 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 423 GEVVKAFVVL-ASQFLShdpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:cd17637 280 GEGIKAVCVLkPGATLT------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
4-488 |
5.16e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 168.57 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLsGACGLQRGDRVAVvLPRVPEWWLV-ILGCIRAGL-IFMPGT----IQMKstDILYRLqmsKAKA 77
Cdd:PRK07788 77 YAELDEQSNALARGL-LALGVRAGDGVAV-LARNHRGFVLaLYAAGKVGArIILLNTgfsgPQLA--EVAARE---GVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 78 IVAGDEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEH 154
Cdd:PRK07788 150 LVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLI--AGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 155 ----SYSSLG-------LKAKMdagwTGLQASDIMWTisdTGW-ILNIlcslmePWALGaCTFVhLLPKFDPLVILKTLS 222
Cdd:PRK07788 228 pepsPLAPLAgllsrvpFRAGE----TTLLPAPMFHA---TGWaHLTL------AMALG-STVV-LRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 SYPIKSMMGAPIVYRMLLQQ--------DLSSYKFphlqnCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS 294
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLgpevlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIAT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 295 -KTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkpirpiGI-FSGYVDNPDKtaANIRGdfwLL--GDRGI 370
Cdd:PRK07788 368 pEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 371 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE-LQ 449
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA------PGAALDEDaIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 815659680 450 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 488
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2-491 |
6.34e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 167.06 E-value: 6.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGC--IRAGLIFMPGTIQMKstDILYRLQMSKAKAIV 79
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALqqLGAVAVLLNTRLSRE--ELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVA----SECPSLRIKLLVSEKSCDgwlnfkklLNEASTthhcvetgsqeasaIYFTSGTSGLPKMAEHS 155
Cdd:PRK03640 105 TDDDFEAKLIPGIsvkfAELMNGPKEEAEIQEEFD--------LDEVAT--------------IMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 Y---------SSLGLkakmdagwtGLQASDiMWTISDTgwILNI--LCSLMEPWALGaCTfVHLLPKFDPLVILKTLSSY 224
Cdd:PRK03640 163 YgnhwwsavgSALNL---------GLTEDD-CWLAAVP--IFHIsgLSILMRSVIYG-MR-VVLVEKFDAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 225 PIkSMMGApiVYRML--LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcmvSKTMKIKPG 302
Cdd:PRK03640 229 GV-TIISV--VSTMLqrLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETA-----SQIVTLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 303 YM----GTAAS-CYDVQI-IDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRgDFWL-LGDRGIKDEDG 375
Cdd:PRK03640 301 DAltklGSAGKpLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNREDATRETFQ-DGWFkTGDIGYLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshdPEQltkELQQHVKSV 455
Cdd:PRK03640 375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV----TEE---ELRHFCEEK 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKM 491
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
4-481 |
1.03e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 168.97 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FmpgtiqmKSTDILYRLQMSKAK 76
Cdd:PRK10524 87 FRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF-------ASHSLAARIDDAKPV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIV---AG-------------DEVIQE----------VDTVASECP----------SLRIKLLVSEKSCDgWLNfkklln 120
Cdd:PRK10524 159 LIVsadAGsrggkvvpykpllDEAIALaqhkprhvllVDRGLAPMArvagrdvdyaTLRAQHLGARVPVE-WLE------ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 121 eastthhcvetgSQEASAIYFTSGTSGLPKMAEHS---YSsLGLKAKMDAGWTGlQASDIMWTISDTGWILNILCSLMEP 197
Cdd:PRK10524 232 ------------SNEPSYILYTSGTTGKPKGVQRDtggYA-VALATSMDTIFGG-KAGETFFCASDIGWVVGHSYIVYAP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 198 WALGACTFVH----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLlPETLENW 270
Cdd:PRK10524 298 LLAGMATIMYeglpTRP--DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEPL-DEPTASW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 271 RAQT-GLDIRESYGQTETGLTCMVS----KTMKIKPGYMGTAASCYDVQIIDDK-GNVLPPGTEGDIGIRvkPIRPIGIF 344
Cdd:PRK10524 375 ISEAlGVPVIDNYWQTETGWPILAIargvEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE--GPLPPGCM 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 345 SgyvdnpdktaaNIRGD-------FWLLGDR--------GIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAV 409
Cdd:PRK10524 453 Q-----------TVWGDddrfvktYWSLFGRqvystfdwGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAV 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 410 VETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:PRK10524 522 AEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
21-485 |
1.09e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 165.93 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 21 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqEVDTVASECPSLRI 100
Cdd:PRK07787 39 AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLG------PAPDDPAGLPHVPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 101 KLlvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL--GLKAKMDAgWTglqasdim 178
Cdd:PRK07787 113 RL------------------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIaaDLDALAEA-WQ-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 179 WTISDT-----------GWILNILCSLMepwaLGAcTFVHLLpKFDPLVILKTLSSYpiKSMM-GAPIVYRMLLQQDLSS 246
Cdd:PRK07787 166 WTADDVlvhglplfhvhGLVLGVLGPLR----IGN-RFVHTG-RPTPEAYAQALSEG--GTLYfGVPTVWSRIAADPEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 247 YKFPHLQNCVTvGESLLPET-LENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP 325
Cdd:PRK07787 238 RALRGARLLVS-GSAALPVPvFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 326 GTE--GDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR-ANDIINSSGYRIGPSEVEN 401
Cdd:PRK07787 317 DGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 402 ALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQLTkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:PRK07787 392 ALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
....
gi 815659680 482 AKLR 485
Cdd:PRK07787 465 KQLL 468
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
23-486 |
1.83e-45 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 166.55 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 23 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLR-IK 101
Cdd:cd17642 65 GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKtII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 102 LLVSEKSCDGWL---NFKK-----LLNEASTTHHCVETGSQeASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQ 173
Cdd:cd17642 145 ILDSKEDYKGYQclyTFITqnlppGFNEYDFKPPSFDRDEQ-VALIMNSSGSTGLPKGVQLTHKNI--VARFSHARDPIF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 174 ASDIMWTISdtgwILNILcslmePWALG----------ACTF-VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 242
Cdd:cd17642 222 GNQIIPDTA----ILTVI-----PFHHGfgmfttlgylICGFrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 243 DL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID-DK 319
Cdd:cd17642 293 TLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 320 GNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 398
Cdd:cd17642 373 GKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 399 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSVTAPYKYPR-KIEFVLNLPKTVT 476
Cdd:cd17642 448 LESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAG------KTMTeKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLT 521
|
490
....*....|
gi 815659680 477 GKIQRAKLRD 486
Cdd:cd17642 522 GKIDRRKIRE 531
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2-486 |
2.10e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 165.75 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVvLPRVPEWWLVI-LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVa 80
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 GDEVIQevdtvASECPSLRIKLLVSEKSCDGWLNFKKLLNEAstthhcvetgsqeASAIYFTSGTSGLPKMA-------E 153
Cdd:PRK09088 100 GDDAVA-----AGRTDVEDLAAFIASADALEPADTPSIPPER-------------VSLILFTSGTSGQPKGVmlsernlQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 154 HSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNILCSLMEpwalGACTFVHllPKFDPLVILKTLS--SYPIKSMMG 231
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHII---GLITSVRPVLAV----GGSILVS--NGFEPKRTLGRLGdpALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 232 APIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQtGLDIRESYGQTETGLTCMVSKTMKI---KPGYMGTA 307
Cdd:PRK09088 233 VPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDI 386
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLR-GP----NLSPGYWRRPQATARAFTGDGWFrTGDIARRDADGFFWVVDRKKDM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 387 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIE 466
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|
gi 815659680 467 FVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRD 481
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
4-486 |
2.83e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 166.71 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK05605 60 YAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 V---IQE------VDTVAS-----------------ECPSLRIKLLVSEKSCDGWLNFKKLLNEA----STTHHCVETGS 133
Cdd:PRK05605 139 VaptVERlrrttpLETIVSvnmiaampllqrlalrlPIPALRKARAALTGPAPGTVPWETLVDAAiggdGSDVSHPRPTP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 134 QEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASD-IMWTI----SDTGWILNILCSLMepwaLGAcTFVh 207
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpGLGDGPeRVLAAlpmfHAYGLTLCLTLAVS----IGG-ELV- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 208 LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRES 281
Cdd:PRK05605 293 LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 282 YGQTETGLTCM---VSKTMKikPGYMGTAASCYDVQIID--DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKT 354
Cdd:PRK05605 368 YGLTETSPIIVgnpMSDDRR--PGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVR-------GpqVFKGYWNRPEET 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 355 AANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS 434
Cdd:PRK05605 439 AKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEP 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 815659680 435 QfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK05605 519 G-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2-498 |
3.17e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 166.52 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQ--MKSTDILYRLQMSKAKAIV 79
Cdd:PRK08315 44 WTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEV-----IQEVDTVASEC-------------PSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHcVETGSQEASA--- 138
Cdd:PRK08315 121 AADGFkdsdyVAMLYELAPELatcepgqlqsarlPELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLdpd 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 ----IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---I---------MwtisdtgwILNILCSLmepwALGA 202
Cdd:PRK08315 200 dpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIpvplyhcfgM--------VLGNLACV----THGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 203 CTfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGeSLLP-ETLEnwRAQTGLDIRE 280
Cdd:PRK08315 268 TM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAG-SPCPiEVMK--RVIDKMHMSE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 281 ---SYGQTETG-LTCM----------VSKTMKIKPGYmgtaascyDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--I 343
Cdd:PRK08315 344 vtiAYGMTETSpVSTQtrtddplekrVTTVGRALPHL--------EVKIVDpETGETVPRGEQGELCTR-------GysV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 344 FSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 422
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815659680 423 GEVVKAFVVLasqflsHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ 498
Cdd:PRK08315 489 GEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAAK 559
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2-486 |
4.61e-45 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 162.90 E-value: 4.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 81
Cdd:cd05912 2 YTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqeVDTVASecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAE-----HSY 156
Cdd:cd05912 76 ------LDDIAT---------------------------------------------IMYTSGTTGKPKGVQqtfgnHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLGLKAKMdagwtGLQASDI------MWTISDtgwiLNILC-SLMEpwalgACTfVHLLPKFDPLVILKTLSSYPIKSM 229
Cdd:cd05912 105 SAIGSALNL-----GLTEDDNwlcalpLFHISG----LSILMrSVIY-----GMT-VYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 230 MGAPIVYRMLLQQDLSSYKfPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTETgltCMVSKTMKI-----KPGYM 304
Cdd:cd05912 170 SVVPTMLQRLLEILGEGYP-NNLR-CILLGGGPAPKPLLEQCKEKGIPVYQSYGMTET---CSQIVTLSPedalnKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIIDDKGnvlPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAN 384
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 385 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEQLTKELQQHVksvtAPYKYPRK 464
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVPKK 389
|
490 500
....*....|....*....|..
gi 815659680 465 IEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05912 390 IYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
4-495 |
6.19e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 165.61 E-value: 6.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK08974 51 FRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECP------------------SL------RIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA- 138
Cdd:PRK08974 131 FAHTLEKVVFKTPvkhviltrmgdqlstakgTLvnfvvkYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAf 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPK--MAEH------------SYSSLgLKAKMDAGWTGLQASDImwtisdtgWILNILCSL-MEpwaLGAC 203
Cdd:PRK08974 211 LQYTGGTTGVAKgaMLTHrnmlanleqakaAYGPL-LHPGKELVVTALPLYHI--------FALTVNCLLfIE---LGGQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 204 TFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESY 282
Cdd:PRK08974 279 NLLITNPRDIPGFV-KELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 283 GQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIR 359
Cdd:PRK08974 358 GLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-------GpqVMLGYWQRPEATDEVIK 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 360 gDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLS 438
Cdd:PRK08974 431 -DGWLaTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLT 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 815659680 439 HDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 495
Cdd:PRK08974 510 EE------ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
4-486 |
8.83e-45 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 165.44 E-value: 8.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK08751 53 YREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLR------------------------IKLLVSEKSCDGWLNFKKLLneASTTHHCVETGSQEASAI 139
Cdd:PRK08751 133 FGTTVQQVIADTPVKQvittglgdmlgfpkaalvnfvvkyVKKLVPEYRINGAIRFREAL--ALGRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 140 YF---TSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-----LQASDIMWTISDTGWILNILCSLMEPWALGACTfvHLL-- 209
Cdd:PRK08751 211 AFlqyTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHIFALTANGLVFMKIGGCN--HLIsn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 210 PKFDPLVIlKTLSSYPIKSMMGAPIVYRMLL------QQDLSSYKFPhLQNCVTVGESLlpetLENWRAQTGLDIRESYG 283
Cdd:PRK08751 289 PRDMPGFV-KELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKMT-LGGGMAVQRSV----AERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 284 QTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPirpigIFSGYVDNPDKTAANIRGDF 362
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQ-----VMKGYWKRPEETAKVMDADG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 363 WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDP 441
Cdd:PRK08751 438 WLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDP 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 815659680 442 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK08751 512 ALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
4-486 |
1.13e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 164.99 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD- 82
Cdd:PRK12492 52 YAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 --EVIQEVdtvaseCPSLRIKLLVSEKSCD------GWL---------------------NFKKLLNE-ASTTHHCVETG 132
Cdd:PRK12492 132 fgKLVQEV------LPDTGIEYLIEAKMGDllpaakGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 133 SQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGA---CTFV--- 206
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTAncmCMMVsgn 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 207 HLLPKFDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESY 282
Cdd:PRK12492 286 HNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 283 GQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGD 361
Cdd:PRK12492 366 GLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GP----QVMKGYWQQPEATAEALDAE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 362 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHD 440
Cdd:PRK12492 441 GWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 815659680 441 peqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK12492 521 ------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-485 |
5.87e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 158.21 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM------WTISdtGWILNILCSLMEpwalgACTFVHLLPKF 212
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCF--GSVLGVLACLTH-----GATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 DPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQTETGLT 290
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 291 CMVSKT---MKIKPGYMGTAASCYDVQIIDDKGNVLPP-GTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-L 365
Cdd:cd05917 160 STQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGWLhT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 366 GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT 445
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KEGAELT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 815659680 446 KE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05917 309 EEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
3-490 |
8.67e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.78 E-value: 8.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEwwlVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 79
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPKMAEHSYSS 158
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADES---LGTDMLYSSGTTGRPKGIKRPLPE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKMdaGWTGLQASdiMWTI-SDTGWilniLC-----------SLMEPWALGACTFVhlLPKFDPLVILKTLSSYPI 226
Cdd:PRK13391 179 QPPDTPL--PLTAFLQR--LWGFrSDMVY----LSpaplyhsapqrAVMLVIRLGGTVIV--MEHFDAEQYLALIEEYGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 227 KSMMGAPIVY-RML-------LQQDLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE-TGLTCMVSKTM 297
Cdd:PRK13391 249 THTQLVPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTACDSEEW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 298 KIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKpiRPigiFSgYVDNPDKTAA--NIRGDFWLLGDRGIKDEDG 375
Cdd:PRK13391 324 LAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG--RP---FE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKS 454
Cdd:PRK13391 397 YLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV---DPgPALAAELIAFCRQ 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 815659680 455 VTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 490
Cdd:PRK13391 474 RLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
5-495 |
2.79e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.25 E-value: 2.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 5 RELSENSQQAANVLSG--ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK12406 12 RSFDELAQRAARAAGGlaALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEV-DTVASEC--------PSLRIKLLVSEKSC---------DGWLNfkklLNEASTThhcvETGSQEASAIYfTSG 144
Cdd:PRK12406 92 DLLHGLaSALPAGVtvlsvptpPEIAAAYRISPALLtppagaidwEGWLA----QQEPYDG----PPVPQPQSMIY-TSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 145 TSGLPKmaehsysslglKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEP--------WALGACTFVH---LLPKFD 213
Cdd:PRK12406 163 TTGHPK-----------GVRRAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPlyhsapnaYGLRAGRLGGvlvLQPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 214 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphlqncVTVGESLLP-----ETLENWraqtGLDIRE 280
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPadvkrAMIEWW----GPVIYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 281 SYGQTETGL--TCMVSKTMKiKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpIRPIGIFSgYVDNPDKTAANI 358
Cdd:PRK12406 302 YYGSTESGAvtFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSR---IAGNPDFT-YHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 RGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqfls 438
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV-------- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815659680 439 hDPEQL----TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 495
Cdd:PRK12406 449 -EPQPGatldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2-487 |
4.47e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 159.82 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PRK07470 33 WTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRikLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYF-TSGTSGLPKMAEHSYSSLG 160
Cdd:PRK07470 112 ADFPEHAAAVRAASPDLT--HVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFfTSGTTGRPKAAVLTHGQMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 L-----KAKMDAGWTGLQASDIMWTISDtGWILNILCSLmepwALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIV 235
Cdd:PRK07470 190 FvitnhLADLMPGTTEQDASLVVAPLSH-GAGIHQLCQV----ARGAATVLLPSERFDPAEVWALVERHRVTNLFTVPTI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQqDLSSYKFPH--LQNCVTVGESLLPETLENWRAQTGLDIRESYGQTEtgltcmVSKTMKIKPGYM-----GTAA 308
Cdd:PRK07470 265 LKMLVE-HPAVDRYDHssLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE------VTGNITVLPPALhdaedGPDA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 ---SC------YDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQF 379
Cdd:PRK07470 338 rigTCgfertgMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 380 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLTK-ELQQHVKSVTAP 458
Cdd:PRK07470 413 TGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA------RDGAPVDEaELLAWLDGKVAR 486
|
490 500
....*....|....*....|....*....
gi 815659680 459 YKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PRK07470 487 YKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
4-486 |
5.77e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 159.83 E-value: 5.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 80
Cdd:PRK13295 58 YRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpkt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 --GDEVIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNE--------ASTTHHCVETGSQEASAIYFTSGTSGLPK 150
Cdd:PRK13295 137 frGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLITpaweqepdAPAILARLRPGPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 MAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMM 230
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGA-TAV-LQDIWDPARAAELIRTEGVTFTM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GA-PIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMvsktmkIKPGYMGTAAS 309
Cdd:PRK13295 292 AStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTL------TKLDDPDERAS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 310 CYD--------VQIIDDKGNVLPPGTEGdigiRVKpIRPIGIFSGYVDNPDKTAANIRGdfWL-LGDRGIKDEDGYFQFM 380
Cdd:PRK13295 366 TTDgcplpgveVRVVDADGAPLPAGQIG----RLQ-VRGCSNFGGYLKRPQLNGTDADG--WFdTGDLARIDADGYIRIS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 381 GRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL-ASQflSHDPEQLTKELQQHvkSVTAPY 459
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPrPGQ--SLDFEEMVEFLKAQ--KVAKQY 514
|
490 500
....*....|....*....|....*..
gi 815659680 460 kYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK13295 515 -IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2-485 |
4.06e-42 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 157.23 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI---FMPGtiqMKSTDILYRLQMSKAKAI 78
Cdd:COG1021 51 LSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfALPA---HRRAEISHFAEQSEAVAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEV-----IQEVDTVASECPSLRIKLLVSEKscDGWLNFKKLLNEASTtHHCVETGSQEASAIYFTSGTSGLPKM-- 151
Cdd:COG1021 127 IIPDRHrgfdyRALARELQAEVPSLRHVLVVGDA--GEFTSLDALLAAPAD-LSEPRPDPDDVAFFQLSGGTTGLPKLip 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 152 ---AEHSYSslglkAKMDAGWTGLQASDIMwtisdtgwilniLCSL-------------MEPWALGACtfVHLLPKFDPL 215
Cdd:COG1021 204 rthDDYLYS-----VRASAEICGLDADTVY------------LAALpaahnfplsspgvLGVLYAGGT--VVLAPDPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 216 VILK-------TLSSypiksmMGAPIVYRML-----LQQDLSSYKFphLQncvtVGESLLPETLENwRAQTGLDIR--ES 281
Cdd:COG1021 265 TAFPlierervTVTA------LVPPLALLWLdaaerSRYDLSSLRV--LQ----VGGAKLSPELAR-RVRPALGCTlqQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 282 YGQTEtGLTCM---------VSKTMkikpgymGTAASCYD-VQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVD 349
Cdd:COG1021 332 FGMAE-GLVNYtrlddpeevILTTQ-------GRPISPDDeVRIVDEDGNPVPPGEVGELLTR-------GpyTIRGYYR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 350 NPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKA 428
Cdd:COG1021 397 APEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 815659680 429 FVVLasqflshDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:COG1021 477 FVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
5-414 |
3.41e-41 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 152.42 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 5 RELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKAKA 77
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------LDPAYpaeRLAFiledAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 78 IVAGDEVIQEVDTVASECPSLRIKLLVSEKSCdgwlnfkkllneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 157
Cdd:TIGR01733 76 LLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLglkAKMdAGWT----GLQASDIMW---TIS-DTgwilnilcSLME---PWALGACTFVHL--LPKFDPLVILKTLSSY 224
Cdd:TIGR01733 144 SL---VNL-LAWLarryGLDPDDRVLqfaSLSfDA--------SVEEifgALLAGATLVVPPedEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 225 PIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQTGlDIR--ESYGQTETGLTCMVSKTMKIKPG 302
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGP-GARliNLYGPTETTVWSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 303 YM-----GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAAN-IRGDFWLL--------GDR 368
Cdd:TIGR01733 289 REspvpiGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGDL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 815659680 369 GIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAV 414
Cdd:TIGR01733 364 VRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2-487 |
5.02e-41 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 154.75 E-value: 5.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDtvasecpSLRIKLLV-SEKSCDGWLNFKKLLN---EASTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHS 155
Cdd:PLN02330 135 DTNYGKVK-------GLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGISKgvMLTHR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 ysslGLKAKMDAGWTGLqASDIMWTISDTGWI--------LNILCSLMEPWALgactfVHLLPKFDPLVILKTLSSYPIK 227
Cdd:PLN02330 208 ----NLVANLCSSLFSV-GPEMIGQVVTLGLIpffhiygiTGICCATLRNKGK-----VVVMSRFELRTFLNALITQEVS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 228 SmmgAPIVYRMLL---------QQDLSSYKfphLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETGLTCMV---- 293
Cdd:PLN02330 278 F---APIVPPIILnlvknpiveEFDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLThgdp 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 294 SKTMKI-KPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGI 370
Cdd:PLN02330 352 EKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDGWLhTGDIGY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 371 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQ 450
Cdd:PLN02330 427 IDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV-----INPKAKESEEDILN 501
|
490 500 510
....*....|....*....|....*....|....*..
gi 815659680 451 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PLN02330 502 FVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
135-481 |
7.21e-41 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 149.57 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 135 EASAIYFTSGTSGLPK--MAEHSYSSLGLKAKMDAGwtGLQASDIMWTIS----DTGWILNILCSLMEpwalGACTFVHL 208
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTLRAAAAWADCA--DLTEDDRYLIINpffhTFGYKAGIVACLLT----GATVVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 209 LpkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE 286
Cdd:cd17638 75 V--FDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 287 TGLTCM---------VSKTMkikpgymGTAASCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAAN 357
Cdd:cd17638 153 AGVATMcrpgddaetVATTC-------GRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 358 IRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqf 436
Cdd:cd17638 211 IDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR--- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 815659680 437 lshDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:cd17638 288 ---PGVTLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
208-486 |
3.66e-39 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 148.29 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 208 LLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM--LLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQ 284
Cdd:cd05929 199 LMEKFDPEEFLRLIERYRVTFAQFVPtMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 285 TE-TGLTCMVSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigifSGYVDNPDKTAANIRGDFW 363
Cdd:cd05929 279 TEgQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 364 -LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfLSHDPE 442
Cdd:cd05929 352 sTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP--GADAGT 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 815659680 443 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
3-486 |
6.23e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 148.74 E-value: 6.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK06164 37 SRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 --------EVIQEVDTvaSECPSLRIKLLVSEKSCD-------GWLNFKKLLNEASTTHHCVETGSQEASAIYFT-SGTS 146
Cdd:PRK06164 116 gfkgidfaAILAAVPP--DALPPLRAIAVVDDAADAtpapapgARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 147 GLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMwtisdtgwilniLCSLmePW-----------ALGACTFVHLLPKFDPL 215
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIARAYGYDPGAVL------------LAAL--PFcgvfgfstllgALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 216 VILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCvtvG-ESLLP--ETLENWRAQTGLDIRESYGQTEtgLTCM 292
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF---GfASFAPalGELAALARARGVPLTGLYGSSE--VQAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 293 VS-------KTMKIKPGymGTAASC-YDVQIID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFW 363
Cdd:PRK06164 335 VAlqpatdpVSVRIEGG--GRPASPeARVRARDpQDGALLPDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 364 L-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPE 442
Cdd:PRK06164 408 FrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDG-ASPDEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 815659680 443 qltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG---KIQRAKLRD 486
Cdd:PRK06164 486 ----GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-485 |
8.00e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 144.55 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYF-TSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVHLLPK--FDP 214
Cdd:cd05944 5 AAYFhTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAgyRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 215 LV---ILKTLSSYPIKSMMGAPIVYRMLLQ----QDLSSYKFphlqncVTVGESLLPETLEN-WRAQTGLDIRESYGQTE 286
Cdd:cd05944 84 GLfdnFWKLVERYRITSLSTVPTVYAALLQvpvnADISSLRF------AMSGAAPLPVELRArFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 287 TglTCMVSKTMK---IKPGYMGTAASCYDVQI--IDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIrGD 361
Cdd:cd05944 158 A--TCLVAVNPPdgpKRPGSVGLRLPYARVRIkvLDGVGRLLRDCAPDEVGEIC--VAGPGVFGGYLYTEGNKNAFV-AD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 362 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsQFLSHD 440
Cdd:cd05944 233 GWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK-PGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 815659680 441 PEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05944 312 EEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
3-487 |
1.37e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 147.79 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK08162 45 TWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDTVASECPSLRIkLLV-------SEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MA 152
Cdd:PRK08162 124 EFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKgvVY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 153 EHSYSSLGLKAKMDAgWTGLQASDIMWTISD---TGWilnilCSlmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKS 228
Cdd:PRK08162 203 HHRGAYLNALSNILA-WGMPKHPVYLWTLPMfhcNGW-----CF---PWTVAARAGTNVcLRKVDPKLIFDLIREHGVTH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 229 MMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENwRAQTGLDIRESYGQTETgltcmvsktmkikpgYmGTA 307
Cdd:PRK08162 274 YCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTET---------------Y-GPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDkgnvLPPGTEGDI------------GIRV------KPI----RPIG--------IFSGYVDNPDKTAAN 357
Cdd:PRK08162 337 TVCAWQPEWDA----LPLDERAQLkarqgvryplqeGVTVldpdtmQPVpadgETIGeimfrgniVMKGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 358 IRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqfl 437
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK---- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 815659680 438 shDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDK 487
Cdd:PRK08162 489 --DGASATEeEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2-484 |
2.36e-38 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 145.93 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI---FMPGtiqMKSTDILYRLQMSKAKAI 78
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS---HRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEvIQEVD------TVASECPSLRIKLLvsekscdgwlnfkkllneastthhcvetgsqeasaiyfTSGTSGLPKMA 152
Cdd:cd05920 117 IVPDR-HAGFDhralarELAESIPEVALFLL--------------------------------------SGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 153 EHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCslmePWALGACTF---VHLLPKFDPLVILKTLSSYPIKSM 229
Cdd:cd05920 158 PRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAC----PGVLGTLLAggrVVLAPDPSPDAAFPLIEREGVTVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 230 MGAPIVYRMLLQQ------DLSSYKFphLQncvtVGESLLPETL-ENWRAQTGLDIRESYGQTEtGLTCM--VSKTMKIK 300
Cdd:cd05920 234 ALVPALVSLWLDAaasrraDLSSLRL--LQ----VGGARLSPALaRRVPPVLGCTLQQVFGMAE-GLLNYtrLDDPDEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 301 PGYMGTAASCYD-VQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGY 376
Cdd:cd05920 307 IHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 377 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVKSV- 455
Cdd:cd05920 380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERg 453
|
490 500
....*....|....*....|....*....
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05920 454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
4-487 |
2.45e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 146.18 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagde 83
Cdd:PRK06145 30 YAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVasecPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:PRK06145 105 VDEEFDAI----VALETPKIVIDAAAQADSRRLAQGGLEIPPQAAV--APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWTGLQASDIMWTIsdtGWILNI-LCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQ 241
Cdd:PRK06145 179 IDHVIALGLTASERLLVV---GPLYHVgAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 242 QDLSSYKFPHLQNCVTVGESLlPETL--ENWRAQTGLDIRESYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIID 317
Cdd:PRK06145 256 PDRDRFDLDSLAWCIGGGEKT-PESRirDFTRVFTRARYIDAYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIAD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 318 DKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPS 397
Cdd:PRK06145 335 GAGRWLPPNMKGEICMRGPKVT-----KGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 398 EVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVT 476
Cdd:PRK06145 410 EVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLE------ALDRHCRQRLASFKVPRQLKVRDELPRNPS 483
|
490
....*....|.
gi 815659680 477 GKIQRAKLRDK 487
Cdd:PRK06145 484 GKVLKRVLRDE 494
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2-484 |
5.14e-38 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 144.31 E-value: 5.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQMskAKAI 78
Cdd:cd05945 17 LTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP-------LDASSpaeRIRE--ILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEVIQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSS 158
Cdd:cd05945 87 AKPALLIADGDDNA---------------------------------------------YIIFTSGSTGRPKGVQISHDN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LglkakmdagwtglqASDIMWTISDTGWI----------LNILCSLME---PWALGACtfVHLLPK---FDPLVILKTLS 222
Cdd:cd05945 122 L--------------VSFTNWMLSDFPLGpgdvflnqapFSFDLSVMDlypALASGAT--LVPVPRdatADPKQLFRFLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 SYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETGLTCMVSK-TMKI 299
Cdd:cd05945 186 EHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEvTPEV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 300 KPGY----MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTA-ANIRGDFWLL---GDRG 369
Cdd:cd05945 266 LDGYdrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPEKTAaAFFPDEGQRAyrtGDLV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 370 IKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIssPDPVRGEVVK--AFVVLAsqflSHDPEQLTKE 447
Cdd:cd05945 339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV--PKYKGEKVTEliAFVVPK----PGAEAGLTKA 412
|
490 500 510
....*....|....*....|....*....|....*..
gi 815659680 448 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05945 413 IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
70-487 |
1.06e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 145.29 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 70 LQMSKAKAIVAGDEVIQEVDTVASECP-SLRIKLLVSEKScdgwlnfkKLLNEASTTHHC---VETGSQEASAIYFTSGT 145
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCPqATRIVAWTDEDH--------DLTVEVLIAAHAgqrPEPTGRKGRVILLTSGT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 146 SGLPKMAEHSYS--SLGLKAKMD-AGWTGLQASDIMWTISDTGWILNILCSlmepwALGACTFVhLLPKFDPLVILKTLS 222
Cdd:PRK13382 208 TGTPKGARRSGPggIGTLKAILDrTPWRAEEPTVIVAPMFHAWGFSQLVLA-----ASLACTIV-TRRRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 SYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-KTMK 298
Cdd:PRK13382 282 RHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 299 IKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKtaaNIRGDFWLLGDRGIKDEDGYFQ 378
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQ-----FDGYTSGSTK---DFHDGFMASGDVGYLDENGRLF 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 379 FMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAP 458
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE----TLKQHVRDNLAN 508
|
410 420
....*....|....*....|....*....
gi 815659680 459 YKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2-451 |
2.31e-36 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 140.04 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdiLYrlQMSKAKAIvag 81
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IY--PTSSAEQI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikllvsekscdGWLnfkklLNEASTTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSSLgl 161
Cdd:cd05907 70 -----------------------------AYI-----LNDSEAKALFVEDPDDLATIIY-TSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGLQASDIMWTIS--DTGWILNILCSLMEPWALGACTFVHLLPKfdplVILKTLSSYPIKSMMGAPIVYRML 239
Cdd:cd05907 113 LSNALALAERLPATEGDRHLSflPLAHVFERRAGLYVPLLAGARIYFASSAE----TLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 240 ---LQQDLSS------YKFPHLQNC--VTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAA 308
Cdd:cd05907 189 yaaIKVKAVPglkrklFDLAVGGRLrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAND-I 386
Cdd:cd05907 269 PGVEVRIADD-GEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFLHITGRKKDlI 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 387 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPvrgeVVKAFVVLasqflshDPEQLTKELQQH 451
Cdd:cd05907 334 ITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4-487 |
2.93e-36 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 140.89 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PLN02246 53 YADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPslrIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHS--YSSL 159
Cdd:PLN02246 132 YVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKgvMLTHKglVTSV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWTGLQASDI------MWTIsdtgWILN--ILCSLMepwaLGACtfVHLLPKFDPLVILKTLSSYPIK-SMM 230
Cdd:PLN02246 209 AQQVDGENPNLYFHSDDVilcvlpMFHI----YSLNsvLLCGLR----VGAA--ILIMPKFEIGALLELIQRHKVTiAPF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRM-----LLQQDLSSYKFphlqncVTVGESLLPETLEN-WRAQ-TGLDIRESYGQTETG---LTCMV-SKT-MK 298
Cdd:PLN02246 279 VPPIVLAIakspvVEKYDLSSIRM------VLSGAAPLGKELEDaFRAKlPNAVLGQGYGMTEAGpvlAMCLAfAKEpFP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 299 IKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGY 376
Cdd:PLN02246 353 VKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLNDPEATANTIDKDGWLhTGDIGYIDDDDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 377 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQF-LSHDpeqltkELQQHVKSV 455
Cdd:PLN02246 428 LFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSeITED------EIKQFVAKQ 501
|
490 500 510
....*....|....*....|....*....|..
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PLN02246 502 VVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
4-478 |
5.49e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 140.02 E-value: 5.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTIQMKSTD--ILYRLQMSKAKAIVAG 81
Cdd:PRK07798 31 YAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAV--PVNVNYRYVEdeLRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASECPSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS 155
Cdd:PRK07798 108 REFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 156 ---YSSLGLKAKMdagwTGLQASDiMWTISD-----TGWILNILCSLME---PWAL------GACTFVHLLPKFDPLVIL 218
Cdd:PRK07798 187 difRVLLGGRDFA----TGEPIED-EEELAKraaagPGMRRFPAPPLMHgagQWAAfaalfsGQTVVLLPDVRFDADEVW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfphLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETGL 289
Cdd:PRK07798 262 RTIEREKVNVItivgdaMARPLLdaLEARGPYDLSS-----LFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSETGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 290 tCMVSKTMKIKPGYMG---TAAScyDVQIIDDKGNVLPPGtEGDIGI--RVKPIrPIGifsgYVDNPDKTAAN---IRGD 361
Cdd:PRK07798 337 -GGSGTVAKGAVHTGGprfTIGP--RTVVLDEDGNPVEPG-SGEIGWiaRRGHI-PLG----YYKDPEKTAETfptIDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 362 FW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHD 440
Cdd:PRK07798 408 RYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPD 486
|
490 500 510
....*....|....*....|....*....|....*...
gi 815659680 441 PEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 478
Cdd:PRK07798 487 LA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
23-491 |
5.46e-35 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 137.67 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 23 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVASEcpSLRI-- 100
Cdd:PLN02479 66 SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM----VDQEFFTLAEE--ALKIla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 101 ---------KLLV--SEKSCD----------GWLNFKKLLneastthhcvETGSQE-----------ASAIYFTSGTSGL 148
Cdd:PLN02479 140 ekkkssfkpPLLIviGDPTCDpkslqyalgkGAIEYEKFL----------ETGDPEfawkppadewqSIALGYTSGTTAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 149 PKMAEHSYSSLGLKAKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGA-CTFVHLLPKFDPLVILKTLSS 223
Cdd:PLN02479 210 PKGVVLHHRGAYLMALSNALIWGMNEGAVyLWTLPMfhcNGWCF--------TWTLAAlCGTNICLRQVTAKAIYSAIAN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 224 YPIKSMMGAPIVYRMLLQQDLSS--YKFPHLQNCVTVGESLLPETLENWrAQTGLDIRESYGQTET-------------- 287
Cdd:PLN02479 282 YGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETygpstvcawkpewd 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 288 GLTCMVSKTMKIKPGYMGTAASCYDVqiIDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIRGDFWLLGD 367
Cdd:PLN02479 361 SLPPEEQARLNARQGVRYIGLEGLDV--VDTKTMKPVPADGKTMGEIV--MRGNMVMKGYLKNPKANEEAFANGWFHSGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 368 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKE 447
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAED 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 815659680 448 LQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDKEWKM 491
Cdd:PLN02479 517 IMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAKAKEM 559
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
21-481 |
7.40e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 136.94 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 21 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRI 100
Cdd:PRK05852 62 RSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 101 KLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA-IYFTSGTSGLPKMAEHSYSSLGlkAKMDAGWTGLQASD--- 176
Cdd:PRK05852 142 NVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAmIMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRLSPrda 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 177 ---IMWTISDTGWILNILCSLMEPWALgactfvhLLP---KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ---DLSSY 247
Cdd:PRK05852 220 tvaVMPLYHGHGLIAALLATLASGGAV-------LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 248 KFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTET----------GLTCMVSKTMKIKPGYMGTAAscyDVQIID 317
Cdd:PRK05852 293 KPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqieGIGQTENPVVSTGLVGRSTGA---QIRIVG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 318 DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGP 396
Cdd:PRK05852 370 SDGLPLPAGAVGEVWLRGTTV-----VRGYLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGEKISP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 397 SEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV-LASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTV 475
Cdd:PRK05852 444 ERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVpRESAPPTAE------ELVQFCRERLAAFEIPASFQEASGLPHTA 517
|
....*.
gi 815659680 476 TGKIQR 481
Cdd:PRK05852 518 KGSLDR 523
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
282-477 |
1.11e-33 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 129.73 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 282 YGQTE-TGLTCMvsktmkikPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNPDK 353
Cdd:cd17636 143 YGQTEvMGLATF--------AALGGGAIGGAgrpsplvQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 354 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL- 432
Cdd:cd17636 210 NARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLk 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 815659680 433 ASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 477
Cdd:cd17636 290 PGASVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2-485 |
1.87e-33 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 131.72 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivag 81
Cdd:cd17649 13 LSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtVASECPSLRIKLLVsEKSCDGWLnfkkllneasTTHHcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd17649 67 ---------LDPEYPAERLRYML-EDSGAGLL----------LTHH----PRQLAYVIY-TSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLL 240
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlQQLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 241 QQ--DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIREsYGQTETGLTCMVSKT---MKIKPGYM--GTAASCYDV 313
Cdd:cd17649 201 EEadRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNA-YGPTEATVTPLVWKCeagAARAGASMpiGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 314 QIIDDKGNVLPPGTEGD--IGIRvkpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRA 383
Cdd:cd17649 280 YILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 384 NDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVL-ASQFLSHDPEQltkeLQQHVKSVTAPYKYP 462
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQ----LRTALRASLPDYMVP 427
|
490 500
....*....|....*....|...
gi 815659680 463 RKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd17649 428 AHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
2-485 |
1.95e-33 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 132.47 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd17651 21 LTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEVIQEVDTVASecpslrikllvsekscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 161
Cdd:cd17651 100 PALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 -------KAKMDAGWTGLQASDIMWTISdTGWILNILCSlmepwalGACtfVHLLP---KFDPLVILKTLSSYPI-KSMM 230
Cdd:cd17651 164 lvawqarASSLGPGARTLQFAGLGFDVS-VQEIFSTLCA-------GAT--LVLPPeevRTDPPALAAWLDEQRIsRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRMLLQQDLSSYKFPHLQNCVTVGESL-LPETLENW-RAQTGLDIRESYGQTETglTCMVSKTMKIKPGYMGTAA 308
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREFcAGLPGLRLHNHYGPTET--HVVTALSLPGDPAAWPAPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SC------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDG 375
Cdd:cd17651 312 PIgrpidnTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAERFVPDpfvpgarMYRTGDLARWLPDG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlASQFLSHDPEqltkELQQHVKSV 455
Cdd:cd17651 387 ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV-GDPEAPVDAA----ELRAALATH 461
|
490 500 510
....*....|....*....|....*....|
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
4-485 |
3.82e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 131.44 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRgdRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK07638 29 YKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVasECPSLRIkllvsekscDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSlglka 163
Cdd:PRK07638 107 KLNDLPDE--EGRVIEI---------DEW---KRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 kmdagWT-GLQASDIMWTISDTGWILnILCSLMEPWAL-GACT------FVHLLPKFDPLVILKTLSSYPIKSMMGAPIV 235
Cdd:PRK07638 168 -----WLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLyGAIStlyvgqTVHLMRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQQDlssyKFPhlQNCVTV---GESLLPETLEnwRAQTG---LDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAA 308
Cdd:PRK07638 242 LESLYKEN----RVI--ENKMKIissGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSfVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SCYDVQIIDDKGNVLPPGTEGDIGIRvKPIRpigiFSGYVdNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDII 387
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYI-IGGVLARELNADGWMtVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 388 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEF 467
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHF 458
|
490
....*....|....*...
gi 815659680 468 VLNLPKTVTGKIQRAKLR 485
Cdd:PRK07638 459 VDEIPYTNSGKIARMEAK 476
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
6-484 |
5.04e-33 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 131.09 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 6 ELSENSQQAANVLSGacGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD--E 83
Cdd:cd05923 34 LRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVdaQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECpsLRIKLLVSEKSCDgwlNFKKLLNEASTthhcvetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:cd05923 112 VMDAIFQSGVRV--LALSDLVGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWTGLQASDimwtisdtgwiLNILCSLMEPW-----------ALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGA 232
Cdd:cd05923 180 LFMSTQAGLRHGR-----------HNVVLGLMPLYhvigffavlvaALALDGTYVVVEEFDPADALKLIEQERVTSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 233 PIVYRMLLQQDL-SSYKFPHLQNCVTVGESL---LPETLENWRAQTGLDIresYGQTETgltcMVSKTMK-IKPGYMGTA 307
Cdd:cd05923 249 PTHLDALAAAAEfAGLKLSSLRHVTFAGATMpdaVLERVNQHLPGEKVNI---YGTTEA----MNSLYMRdARTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDKGNV---LPPGTEGDIgirVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAN 384
Cdd:cd05923 322 GFFSEVRIVRIGGSPdeaLANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 385 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltkELQQHVK-SVTAPYKYPR 463
Cdd:cd05923 399 DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRaSELADFKRPR 472
|
490 500
....*....|....*....|.
gi 815659680 464 KIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05923 473 RYFFLDELPKNAMNKVLRRQL 493
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
11-485 |
2.70e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 127.22 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 11 SQQAANVLSGACGL-----QRGDRVAVVLPRvPEW---WLVILGCirAGLIFMPgtiqmkstdILYRLQMSKAKAIVagd 82
Cdd:PLN02860 36 HEFVDGVLSLAAGLlrlglRNGDVVAIAALN-SDLyleWLLAVAC--AGGIVAP---------LNYRWSFEEAKSAM--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDTVASE-------------CPSLRIKLLVSEKSCDGWLNFKKLLN-EASTTHHCVETGSQEASA------IYFT 142
Cdd:PLN02860 101 LLVRPVMLVTDEtcsswyeelqndrLPSLMWQVFLESPSSSVFIFLNSFLTtEMLKQRALGTTELDYAWApddavlICFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 143 SGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIS---DTGWILNILCSLMepwaLGACtfvH-LLPKFDPLVIL 218
Cdd:PLN02860 181 SGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAplcHIGGLSSALAMLM----VGAC---HvLLPKFDAKAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIKSMMGAPIVYRMLL---QQDLSSYKFPHLQNCVTVGES----LLPETLENW-RAQtgldIRESYGQTET--G 288
Cdd:PLN02860 254 QAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSlssrLLPDAKKLFpNAK----LFSAYGMTEAcsS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 289 LTCMV--SKTMKIKPGYMGTAASCYDvQIIDDKGNVL----PPGTEgdIGIRVKPIRPIG-IFS-------GYVDNPDKT 354
Cdd:PLN02860 330 LTFMTlhDPTLESPKQTLQTVNQTKS-SSVHQPQGVCvgkpAPHVE--LKIGLDESSRVGrILTrgphvmlGYWGQNSET 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 355 AANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL- 432
Cdd:PLN02860 407 ASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLr 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815659680 433 -------ASQFLSHDPEQLTKE-LQQHV--KSVTApYKYPRKieFVLN---LPKTVTGKIQRAKLR 485
Cdd:PLN02860 487 dgwiwsdNEKENAKKNLTLSSEtLRHHCreKNLSR-FKIPKL--FVQWrkpFPLTTTGKIRRDEVR 549
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
4-484 |
3.35e-31 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 125.90 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:cd17655 25 YRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQevdtvasecpslrikLLVSEKSCDgWLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS-----Y 156
Cdd:cd17655 104 LQP---------------PIAFIGLID-LLDEDTIYHEESENLEPVSKSDDLAYVIY-TSGSTGKPKgvMIEHRgvvnlV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLGLKAKMDAGWTGLQASDIMWTISDTgwilnilcSLMEPWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAP 233
Cdd:cd17655 167 EWANKVIYQGEHLRVALFASISFDASVT--------EIFASLLSGNT--LYIVRKetvLDGQALTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 234 IVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENW--RAQTGLDIRESYGQTETGLTCMV-----SKTMKIKPgYMGT 306
Cdd:cd17655 237 AHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqyepETDQQVSV-PIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 307 AASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKD-------EDGYFQF 379
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDDPFVPGERMYRTgdlarwlPDGNIEF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 380 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEQLTKELQQHVKSVTAPy 459
Cdd:cd17655 389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL---PVAQLREFLARELPDYMIP- 464
|
490 500
....*....|....*....|....*
gi 815659680 460 KYPRKIEfvlNLPKTVTGKIQRAKL 484
Cdd:cd17655 465 SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-487 |
3.83e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 126.75 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtIQMKST--DILYRLQMSKAKAIV 79
Cdd:COG1022 41 LTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP--IYPTSSaeEVAYILNDSGAKVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGD-EVIQEVDTVASECPSLRiKLLV----SEKSCDGWLNFKKLLNEASTTHH--CVETGSQEASA-----IYFTSGTSG 147
Cdd:COG1022 118 VEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLALGREVADpaELEARRAAVKPddlatIIYTSGTTG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 148 LPKMAEHSYSSLglkakmdagWTGLQASDIMWTISDTGWILNILcslmePWA-------------LGAC--------TFV 206
Cdd:COG1022 197 RPKGVMLTHRNL---------LSNARALLERLPLGPGDRTLSFL-----PLAhvfertvsyyalaAGATvafaespdTLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 207 HLLPKFDPLVIL---------------KTLSSYPIKSM-----MGAPIVYRMLLQQDLS---SYKFPH------------ 251
Cdd:COG1022 263 EDLREVKPTFMLavprvwekvyagiqaKAEEAGGLKRKlfrwaLAVGRRYARARLAGKSpslLLRLKHaladklvfsklr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 252 ------LQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAAScyDVQI-IDDKGNVLp 324
Cdd:COG1022 343 ealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLP--GVEVkIAEDGEIL- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 325 pgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDII-NSSGYRIGPSEVENA 402
Cdd:COG1022 419 -------------VRGPNVMKGYYKNPEATAEAFDADGWLHtGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 403 LMEHP----AVV--E-----TAVIsSPDPvrgEVVK--------AFVVLASqfLSHDPEqLTKELQQHVKSVTApyKYPR 463
Cdd:COG1022 486 LKASPlieqAVVvgDgrpflAALI-VPDF---EALGewaeenglPYTSYAE--LAQDPE-VRALIQEEVDRANA--GLSR 556
|
570 580 590
....*....|....*....|....*....|....*.
gi 815659680 464 --KI-EFVLnLPK---------TVTGKIQRAKLRDK 487
Cdd:COG1022 557 aeQIkRFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
138-481 |
4.38e-31 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 122.75 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYFTSGTSGLPKMAEHSYSSLGLKAKMdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTF-----VHLLPKF 212
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhgglcVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 DPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVG-ESLLPETLENWRAQTGLDIRESYGQTETG-LT 290
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgSRAIAADVRFIEATGLTNTAQVYGLSETGtAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 291 CMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 370
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSP-----ANMLGYWNNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 371 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshDPEQLTKELQQ 450
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|.
gi 815659680 451 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:cd17635 310 TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
141-487 |
5.49e-31 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 122.05 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 141 FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDimwtisdtGWilniLCSLmeP------------WALGACTFVhL 208
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD--------SW----LLSL--PlyhvgglailvrSLLAGAELV-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 209 LPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETG 288
Cdd:cd17630 72 LERNQAL--AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRA-VLLGGAPIPPELLERAADRGIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 289 LTcmvsktmkikpgymgTAASCYDVQIIDDKGNVLPpgtegDIGIRVKP-----IRPIGIFSGYVDNPDKTAANIRGdfW 363
Cdd:cd17630 149 SQ---------------VATKRPDGFGRGGVGVLLP-----GRELRIVEdgeiwVGGASLAMGYLRGQLVPEFNEDG--W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 364 L-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshDPE 442
Cdd:cd17630 207 FtTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 815659680 443 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
4-484 |
2.95e-30 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 123.15 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM--SKAKAI 78
Cdd:cd17646 26 YRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP-------LDPGYpadRLAYmlADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VagdeVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSY 156
Cdd:cd17646 98 V----VLTTADLAARLPAGGDVALLGDE-----------ALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKgvMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SS---LGLKAK--MDAGWTGLQASDIMWTISdtGW-ILnilcslmepWAL--GACTFV-----HLlpkfDPLVILKTLSS 223
Cdd:cd17646 163 IVnrlLWMQDEypLGPGDRVLQKTPLSFDVS--VWeLF---------WPLvaGARLVVarpggHR----DPAYLAALIRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 224 YPIKSMMGAPIVYRMLLQQDLSSyKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE-----TGLTCMVSKTMK 298
Cdd:cd17646 228 HGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaidvTHWPVRGPAETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 299 IKP-GYMGTAASCYdvqIIDDKGNVLPPGTEGDI---GIRVKpirpigifSGYVDNPDKTAANIRGD-------FWLLGD 367
Cdd:cd17646 307 SVPiGRPVPNTRLY---VLDDALRPVPVGVPGELylgGVQLA--------RGYLGRPALTAERFVPDpfgpgsrMYRTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 368 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEqltkE 447
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTA----A 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 815659680 448 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17646 452 LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
4-484 |
3.47e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 122.69 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 83
Cdd:cd12117 25 YAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viQEVDTVASECPSLRIKLLVSEKSCDGwlnfkklLNEASTthhcvetGSQEASA-IYFTSGTSGLPK--MAEHsYSSLG 160
Cdd:cd12117 101 --DRSLAGRAGGLEVAVVIDEALDAGPA-------GNPAVP-------VSPDDLAyVMYTSGSTGRPKgvAVTH-RGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 LKakMDAGWTGLQASDIMWTISDTGWIlnilCSLMEPW-AL--GACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 234
Cdd:cd12117 164 LV--KNTNYVTLGPDDRVLQTSPLAFD----ASTFEIWgALlnGAR--LVLAPKgtlLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETGL--TCMVsktmkIKPGYM------- 304
Cdd:cd12117 236 LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTftTSHV-----VTELDEvagsipi 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTA----ANIRGD---FWLLGDRGIKDED 374
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELyvgGD--------GLALGYLNRPALTAerfvADPFGPgerLYRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 375 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD-PVRGEVVkAFVVlASQFLSHDpeqltkELQQHVK 453
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-AYVV-AEGALDAA------ELRAFLR 452
|
490 500 510
....*....|....*....|....*....|.
gi 815659680 454 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
4-485 |
4.99e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 123.35 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:PRK05620 41 FAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLRIKLLVSEKSCDG----------WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 153
Cdd:PRK05620 121 LAEQLGEILKECPCVRAVVFIGPSDADSaaahmpegikVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 154 HSYSSLGLKAkmdagwTGLQASDIMWTISDTGW-----ILNIL--CSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPI 226
Cdd:PRK05620 201 YSHRSLYLQS------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGT-PLVFPGPDLSAPTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 227 KSMMGAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTmkiKPGYMG 305
Cdd:PRK05620 274 RVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PSGVSG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 306 TAASCYDV-----------QIIDDkGNVLPPG--TEGDIGIRvKPIRPIGIFSGYVDNPDKTAANIRG------------ 360
Cdd:PRK05620 351 EARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYHSPTEEGGGAASTFRGedvedandrfta 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 361 DFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 439
Cdd:PRK05620 429 DGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI--- 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 815659680 440 DPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK05620 506 EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2-487 |
6.07e-30 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 122.58 E-value: 6.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNfrELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd05932 9 WG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 --DEVIQEVDTVASECPSLRIKLLVSEKSCDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL 159
Cdd:cd05932 86 klDDWKAMAPGVPEGLISISLPPPSAANCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWTGLQASDIMW-----------TISDTGWILNilcSLMEPWALGACTFVHLLPKFDPLVI-----LKTLSS 223
Cdd:cd05932 163 AWAAQAGIEHIGTEENDRMLsylplahvterVFVEGGSLYG---GVLVAFAESLDTFVEDVQRARPTLFfsvprLWTKFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 224 YPIKSMMGA---------PIVYRMLLQQDLSSYKFPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS 294
Cdd:cd05932 240 QGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 295 KTMKIKPGYMGTAAScyDVQI-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKD 372
Cdd:cd05932 319 YPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VRSPALMMGYYKDPEATAEAFTADGFLrTGDKGELD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 373 EDGYFQFMGRANDIINSS-GYRIGPSEVENALMEHPAVVETAVISS--PDPVRGEVVKAFVVLASqfLSHDPEQLTKELQ 449
Cdd:cd05932 383 ADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRA--DAFARAELEASLR 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 815659680 450 QHVKSVTAPYKYPRKIEFVL---------NLPKTVTGKIQRAKLRDK 487
Cdd:cd05932 461 AHLARVNSTLDSHEQLAGIVvvkdpwsidNGILTPTLKIKRNVLEKA 507
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-485 |
2.88e-29 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 121.54 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 80
Cdd:PLN02654 123 YSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITcna 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 ---GDEVIQEVDTV-------ASECPSLRIKLLVSEKSC------------DGWlnFKKLLNEASTTHHCVETGSQEASA 138
Cdd:PLN02654 202 vkrGPKTINLKDIVdaaldesAKNGVSVGICLTYENQLAmkredtkwqegrDVW--WQDVVPNYPTKCEVEWVDAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTFV-HLLPK 211
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTtggymvYTATTFKYAFD-----YKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVfEGAPN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 212 F-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETlenWR------AQTGLDIRES 281
Cdd:PLN02654 355 YpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRwffnvvGDSRCPISDT 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 282 YGQTETGlTCMVSKTMKIKPGYMGTAA-SCYDVQ--IIDDKGNVLppgtEGDIG--IRVKPIRPiGIFS---GYVDNPDK 353
Cdd:PLN02654 432 WWQTETG-GFMITPLPGAWPQKPGSATfPFFGVQpvIVDEKGKEI----EGECSgyLCVKKSWP-GAFRtlyGDHERYET 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 354 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 433
Cdd:PLN02654 506 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 815659680 434 SQFLShdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PLN02654 586 EGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
23-492 |
3.80e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.29 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 23 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQmkstdiLYRlqmskakaivaGDEVIQEVDTVASecpslrikL 102
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE------LHR-----------DDHALAARNTEPA--------L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 103 LVSEKS-CDGW-----LNFKKLLNEAS---TTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSS-LGLKAKMDAGWTGL 172
Cdd:PRK06060 106 VVTSDAlRDRFqpsrvAEAAELMSEAArvaPGGYEPMGGDALAYATY-TSGTTGPPKAAIHRHADpLTFVDAMCRKALRL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 173 QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP-----------KFDPLVilktlssypiksMMGAPIVYRMLLQ 241
Cdd:PRK06060 185 TPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvtpeaaailsaRFGPSV------------LYGVPNFFARVID 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 242 QdLSSYKFPHLQNCVTVGESL---LPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 318
Cdd:PRK06060 253 S-CSPDSFRSLRCVVSAGEALelgLAERLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 319 KGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANirGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 398
Cdd:PRK06060 330 DGTTAGPGVEGDLWVR-GP----AIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 399 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFLShdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 477
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgATID---GSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
490 500
....*....|....*....|
gi 815659680 478 KIQRAKLRDKE-----WKMS 492
Cdd:PRK06060 480 KLVRGALRKQSptkpiWELS 499
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
14-486 |
1.71e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 118.97 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 14 AANVLSgaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA-------GDEVIQ 86
Cdd:PLN03102 53 AASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVdrsfeplAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 87 EVDTVASEcPSLRIKLL----VSEKSCDGWLNFKKLLNEASTTHHCVET-----GSQEASAIYFTSGTSGLPKMAEHSYS 157
Cdd:PLN03102 131 LLSSEDSN-LNLPVIFIheidFPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLGLKA-KMDAGWTGLQASDIMWTISD---TGWILnilcslmePWALGA------CTFVHLLPKfdplvILKTLSSYPIK 227
Cdd:PLN03102 210 GAYLSTlSAIIGWEMGTCPVYLWTLPMfhcNGWTF--------TWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 228 SMMGAPIVYRMLLQQDLS--SYKFPHLQncVTVGESLLPETLENWRAQTGLDIRESYGQTE-TG--LTCM---------V 293
Cdd:PLN03102 277 HMCCVPTVFNILLKGNSLdlSPRSGPVH--VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 294 SKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP---GTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 370
Cdd:PLN03102 355 NQQMELKARQGVSILGLADVDVKNKETQESVPrdgKTMGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 371 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL--ASQFLSHDPEQL-TKE 447
Cdd:PLN03102 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLvTRE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 815659680 448 --LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PLN03102 510 rdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
139-489 |
2.94e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.86 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDImwtisdtgwilnILCSL--------MEPWALGACT--FVHL 208
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDV------------CYVSMplfhsnavMAGWAVALAAgaSIAL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 209 LPKFDPLVILKTLSSYPIKSM--MGAPIVYRmllqqdLSSYKFP-HLQNCVTV--GESLLPETLENWRAQTGLDIRESYG 283
Cdd:PRK07867 225 RRKFSASGFLPDVRRYGATYAnyVGKPLSYV------LATPERPdDADNPLRIvyGNEGAPGDIARFARRFGCVVVDGFG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 284 QTETGLTcmVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGtEGDIGIRVKPIRPIG---------IFSGYVDNPDK 353
Cdd:PRK07867 299 STEGGVA--ITRTPDTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 354 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 433
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 815659680 434 --SQFlshDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 489
Cdd:PRK07867 454 pgAKF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2-484 |
6.47e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 116.24 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEviqEVDTVASECPSLRIKLLvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIY--FTSGTSGLPKMAEHSYSSL 159
Cdd:cd12116 92 DA---LPDRLPAGLPVLLLALA-----------------AAAAAPAAPRTPVSPDDLAYviYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 G--LKAKMDAgwTGLQASDIMWTISDTGWILNILCSLMePWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 234
Cdd:cd12116 152 VnfLHSMRER--LGLGPGDRLLAVTTYAFDISLLELLL-PLLAGAR--VVIAPRetqRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VYRMLL---QQDLSSYKfphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTcmvSKTMKIKPGY----MGTA 307
Cdd:cd12116 227 TWRMLLdagWQGRAGLT-------ALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIW---STAARVTAAAgpipIGRP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 308 ASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQF 379
Cdd:cd12116 297 LANTQVYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 380 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPEQLTKELQQHVKSVTAPY 459
Cdd:cd12116 372 LGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG-AAPDAAALRAHLRATLPAYMVPS 449
|
490 500
....*....|....*....|....*
gi 815659680 460 KYPRKIEFvlnlPKTVTGKIQRAKL 484
Cdd:cd12116 450 AFVRLDAL----PLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
139-481 |
7.27e-28 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 113.27 E-value: 7.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASdimwtiSDTgwILNILCSLMEPWALGACTF-------VHLLPK 211
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW--IESFVCNEDLFNIS------GED--AILAPGPLSHSLFLYGAISalylggtFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 212 FDPLVILKTLSSYPIKSMMGAPivyrMLLQQdLSSYKFPHL--QNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETG 288
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESkiKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 289 LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVlppgtegdIG-IRVK-PIrpigIFSGYVD----NPDKtaanirgdf 362
Cdd:cd17633 150 FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKsEM----VFSGYVRggfsNPDG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 363 WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshdp 441
Cdd:cd17633 209 WMsVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG--------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 815659680 442 EQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:cd17633 280 DKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-484 |
8.42e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 118.34 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDtVASECPSLRIKLLvsekscdgwlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLK 162
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLCLDEP------------ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AKMDAGWTGLQASDIMWTISDTGWILNILcslMEPWALGACTFVHLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRML 239
Cdd:PRK12467 685 VCVIAERLQLAADDSMLMVSTFAFDLGVT---ELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQAL 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 240 LQQDLSSYKFPhlQNCVTV-GESLLPETLENWRA-QTGLDIRESYGQTETglTCMVS------KTMKIKPGYMGTAASCY 311
Cdd:PRK12467 762 LQASRVALPRP--QRALVCgGEALQVDLLARVRAlGPGARLINHYGPTET--TVGVStyelsdEERDFGNVPIGQPLANL 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 312 DVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRA 383
Cdd:PRK12467 838 GLYILDHYLNPVPVGVVGELYIGGA-----GLARGYHRRPALTAERFVPDpfgadggrLYRTGDLARYRADGVIEYLGRM 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 384 NDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPR 463
Cdd:PRK12467 913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPA 991
|
490 500
....*....|....*....|.
gi 815659680 464 KIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK12467 992 HLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
12-486 |
1.92e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 12 QQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTV 91
Cdd:PLN02574 77 KSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT--TMNPSSSLGEIKKRVVDCSVGLA----FTSPENV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 92 aSECPSLRIK-LLVSEKscdgwLNFKKLLNEASTTHHCVET----------GSQEASAIYFTSGTSGLPK--MAEHS--Y 156
Cdd:PLN02574 151 -EKLSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEdfdfvpkpviKQDDVAAIMYSSGTTGASKgvVLTHRnlI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLGLKAKMDAGWTGLQASD-IMWTISDTGWILNILCSLMEPWALGACTFVhlLPKFDPLVILKTLSSYPIKSMMGAPIV 235
Cdd:PLN02574 225 AMVELFVRFEASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVV--MRRFDASDMVKVIDRFKVTHFPVVPPI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQ--QDLSSYKFPHLQNCVTVGESLLPETLENW-RAQTGLDIRESYGQTET---GLTCMVSKTMKiKPGYMGTAAS 309
Cdd:PLN02574 303 LMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEStavGTRGFNTEKLS-KYSSVGLLAP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 310 CYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDII 387
Cdd:PLN02574 382 NMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEII 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 388 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKIE 466
Cdd:PLN02574 457 KYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVRKVV 530
|
490 500
....*....|....*....|
gi 815659680 467 FVLNLPKTVTGKIQRAKLRD 486
Cdd:PLN02574 531 FVQSIPKSPAGKILRRELKR 550
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
4-486 |
2.19e-27 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 113.94 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 83
Cdd:cd17653 25 YGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP--------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqeVDTvasECPSLRIKLLVSEKSCdgwlnfkKLlneastthhCVETGSQEASA-IYFTSGTSGLPK--MAEHS----Y 156
Cdd:cd17653 77 ----LDA---KLPSARIQAILRTSGA-------TL---------LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRgvlnY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 SSLGlKAKMDA--GWTGLQASDIMWTISdTGWILNILC--------SLMEPWA--LGACTFVHLLPKFdplvilktLSSY 224
Cdd:cd17653 134 VSQP-PARLDVgpGSRVAQVLSIAFDAC-IGEIFSTLCnggtlvlaDPSDPFAhvARTVDALMSTPSI--------LSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 225 PIKSmmgapivyrmllqqdlssykFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYM 304
Cdd:cd17653 204 SPQD--------------------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD-FW------LLGDRGIKDEDGYF 377
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASKFVPDpFWpgsrmyRTGDYGRWTEDGGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQflshDPEQLTKELQQHVKSvta 457
Cdd:cd17653 337 EFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI----VVNGRLVAFVTPETV----DVDGLRSELAKHLPS--- 405
|
490 500
....*....|....*....|....*....
gi 815659680 458 pYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd17653 406 -YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-485 |
3.00e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 114.84 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 23 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIqevdTVASECPSLRIKL 102
Cdd:cd05915 45 GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL----PLVEAIRGELKTV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 103 LVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPKMAEHSY-------SSLGLKAKMDAGWTGLQA 174
Cdd:cd05915 121 QHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHralvlhsLAASLVDGTALSEKDVVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 175 SDI-MWTISdtGWilnilCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHL 252
Cdd:cd05915 201 PVVpMFHVN--AW-----CLPYAATLVGA-KQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADyLESTGHRLKTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 253 QNCVTVGESLlPETLENWRAQTGLDIRESYGQTET---GLTCMVSKTMKIKPGYMGTAASCYD-VQIIDDKGNVLPPGT- 327
Cdd:cd05915 273 RRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEEEKLTLKAKTgLPIPLVRLRVADEEGr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 328 ----EGDIgIRVKPIRPIGIFSGYVDNPDKTAAN-IRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENA 402
Cdd:cd05915 352 pvpkDGKA-LGEVQLKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 403 LMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLTKELQQHVKSVTAPYKY-PRKIEFVLNLPKTVTGKIQR 481
Cdd:cd05915 431 LMGHPKVKEAAVVAIPHPKWQERPLAVVVP------RGEKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLK 504
|
....
gi 815659680 482 AKLR 485
Cdd:cd05915 505 RALR 508
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-486 |
4.86e-27 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 115.72 E-value: 4.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtIqmkstDILY---RLQM----SK 74
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--L-----DPAYpaeRLAYmledAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 75 AKAIVAGDEViqevdtvASECPSLRIKLLVsekscdgwLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MA 152
Cdd:COG1020 574 ARLVLTQSAL-------AARLPELGVPVLA--------LDALALAAEPATNPPVPVTPDDLAYVIY-TSGSTGRPKgvMV 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 153 EHSysslGLKAKMDA--GWTGLQASDIM---WTIS-DTgwilnilcSLME---PWALGACtfVHLLPK---FDPLVILKT 220
Cdd:COG1020 638 EHR----ALVNLLAWmqRRYGLGPGDRVlqfASLSfDA--------SVWEifgALLSGAT--LVLAPPearRDPAALAEL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 221 LSSYPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETglTCMVSkTMKI 299
Cdd:COG1020 704 LARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTET--TVDST-YYEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 300 KPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAAN-IRGDFWLL--- 365
Cdd:COG1020 779 TPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELyigGA--------GLARGYLNRPELTAERfVADPFGFPgar 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 366 ----GDRGIKDEDGYFQFMGRAND---IinsSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfls 438
Cdd:COG1020 851 lyrtGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA---- 923
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 815659680 439 hDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:COG1020 924 -GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-478 |
1.78e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 110.16 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPK--MAEH--SYSSLGLKAKMDAGwtglQASDIMWTI----SDTGWILNILCSLME---PWA-----LGA 202
Cdd:cd05924 8 ILYTGGTTGMPKgvMWRQedIFRMLMGGADFGTG----EFTPSEDAHkaaaAAAGTVMFPAPPLMHgtgSWTafgglLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 203 CTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfphLQNCVTVGESLLPETLENW-RAQ 273
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMtivgdaMARPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 274 TGLDIRESYGQTETGLT-CMVSKTMKIKPGYMGTAAScyDVQIIDDKGNVLPPGTE--GDIGIR-VKPIrpigifsGYVD 349
Cdd:cd05924 159 PNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 350 NPDKTAANIR---GDFW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEV 425
Cdd:cd05924 230 DEAKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 815659680 426 VKAFVVLASqflSHDPEQltKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 478
Cdd:cd05924 310 VVAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
398-478 |
2.04e-26 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 101.85 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 398 EVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 477
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 815659680 478 K 478
Cdd:pfam13193 76 K 76
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
2-485 |
5.59e-26 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 111.24 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELsensQQAANVLSGAC---GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDIL-YRLQM----- 72
Cdd:PRK10946 49 FSYREL----NQASDNLACSLrrqGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNaYASQIepall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 73 --SKAKAIVAGDEVIqevDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK 150
Cdd:PRK10946 125 iaDRQHALFSDDDFL---NTLVAEHSSLRVVLLLND---DGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 MA-----EHSYSslglkakmdagwtgLQAS-DIMWTISDTGWilniLCSL--------MEPWALG---ACTFVHLLPKFD 213
Cdd:PRK10946 199 LIprthnDYYYS--------------VRRSvEICGFTPQTRY----LCALpaahnypmSSPGALGvflAGGTVVLAPDPS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 214 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphLQncvtVGESLLPETLEnwR---AQTGLDIRESY 282
Cdd:PRK10946 261 ATLCFPLIEKHQVNVTALVPPAVSLWLQaiaeggsrAQLASLKL--LQ----VGGARLSETLA--RripAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 283 GQTEtGLtcmVSKT-MKIKPGYMGTAASCY-----DVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKT 354
Cdd:PRK10946 333 GMAE-GL---VNYTrLDDSDERIFTTQGRPmspddEVWVADADGNPLPQGEVGRLMTR-------GpyTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 355 AANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 433
Cdd:PRK10946 402 ASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 815659680 434 SQFlshDPEQLTKEL-QQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK10946 482 EPL---KAVQLRRFLrEQGI----AEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
133-481 |
1.57e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 108.59 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 133 SQEASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASDIMWTIsdtgwilnILCSLMEPWALGACTFV------ 206
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEI--DREIEAYNEALNCEQDETPI--------VACPVTHSYGLICGVLAaltrgs 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 207 --HLLPKFDPLVILKTLSSYPIKSMMGAPIVY----RMLLQQDlssykfpHLQNCVTVGeSLLPET-LENWRAQTgLDIR 279
Cdd:PRK08308 170 kpVIITNKNPKFALNILRNTPQHILYAVPLMLhilgRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERT-TYMM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 280 ESYGQTETGltCM-VSKTMKiKPGYMGTAASCYDVQIIDDKGNvlpPGtegDIGIRVKpirpigifsgyvdnpDKTAANi 358
Cdd:PRK08308 241 QQYGCSEAG--CVsICPDMK-SHLDLGNPLPHVSVSAGSDENA---PE---EIVVKMG---------------DKEIFT- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 rgdfwllGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfvvlasQFLS 438
Cdd:PRK08308 296 -------KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVIS 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 815659680 439 H---DPEQLTKELQQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:PRK08308 363 HeeiDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-484 |
2.51e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 29 RVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrIKLLVSEKS 108
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG------LASLALDRD 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 109 CDgWLNFkkllneaSTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTI 181
Cdd:PRK12316 4677 ED-WEGF-------PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLvnhlhatGERYELTPDDRVLQFMSFSFDG 4748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 182 SDTGWilnilcslMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGES 261
Cdd:PRK12316 4749 SHEGL--------YHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEA 4820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 262 LLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKP---GYM--GTAASCYDVQIIDDKGNVLPPGTEGDIGIRV 335
Cdd:PRK12316 4821 VAQASYdLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDAcgaAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGG 4900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 336 KpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHP 407
Cdd:PRK12316 4901 E-----GVARGYLERPALTAERFVPDpfgapggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 408 AVVETAVISSPDPVRGEVVkAFVVLASQFLSHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK12316 4976 AVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
4-484 |
2.74e-25 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 108.11 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 83
Cdd:cd17652 15 YAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqeVDtvaSECPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 161
Cdd:cd17652 67 ----LD---PAYPAERIAYMLADARP-----------------ALLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----GL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDAGWT--GLQASDIMWTISDTGWILNILCSLMepwALGACTFVHLLPKfDPLV----ILKTLSSYPIKSMMGAPIV 235
Cdd:cd17652 119 ANLAAAQIAafDVGPGSRVLQFASPSFDASVWELLM---ALLAGATLVLAPA-EELLpgepLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQQDLssykfPHLQNCVTVGESLLPETLENWraQTGLDIRESYGQTETGLTCMVSK---TMKIKPgyMGTAASCYD 312
Cdd:cd17652 195 LAALPPDDL-----PDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVCATMAGplpGGGVPP--IGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 313 VQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----ANIRGD----FWLLGDRGIKDEDGYFQFMGRAN 384
Cdd:cd17652 266 VYVLDARLRPVPPGVPGEL-----YIAGAGLARGYLNRPGLTAerfvADPFGApgsrMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 385 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRK 464
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAA 415
|
490 500
....*....|....*....|
gi 815659680 465 IEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17652 416 FVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
2-487 |
3.74e-25 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 108.66 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEviQEVD---TVASECPSLRIKLLVSEKSC----DGWLNFKKLLNEASTTHHCVETGSQEA----------SAIYFTSG 144
Cdd:cd17641 91 DE--EQVDkllEIADRIPSVRYVIYCDPRGMrkydDPRLISFEDVVALGRALDRRDPGLYERevaagkgedvAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 145 TSGLPKMA--------EHSYSSLGLKAK---------MDAGWTGLQasdiMWTISD---TGWILNILCS---LMEPWALG 201
Cdd:cd17641 169 TTGKPKLAmlshgnflGHCAAYLAADPLgpgdeyvsvLPLPWIGEQ----MYSVGQalvCGFIVNFPEEpetMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 202 ACTFVHLLPK-FDPL---VILKTLSSYPIKSMM-------------------------------GAPIVYRMLLQQdlss 246
Cdd:cd17641 245 GPTFVLLPPRvWEGIaadVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRDR---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 247 YKFPHLQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIiDDKGNVLppg 326
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEIL--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 327 tegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSS-GYRIGPSEVENALM 404
Cdd:cd17641 396 -----------VRSPGVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 405 EHPAVVETAVISSPDP-------VRGEVV------KAFVVLASQFLSHDPEqLTKELQQHVKSVTAPYKYPRKIEFVLNL 471
Cdd:cd17641 465 FSPYIAEAVVLGAGRPyltaficIDYAIVgkwaeqRGIAFTTYTDLASRPE-VYELIRKEVEKVNASLPEAQRIRRFLLL 543
|
570 580
....*....|....*....|....*
gi 815659680 472 PK---------TVTGKIQRAKLRDK 487
Cdd:cd17641 544 YKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
3-495 |
1.73e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 106.76 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVV---LPRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 79
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWYGIMG---IGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVASECPSLRIKLLVSEKS------CDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 153
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAhmpqttLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 154 HSYSSLGLKAKM--DAGWTGLQASDIMWTI----SDTGWILNILCSLMepwalGAcTFVHLLPKFDPLVILKTLSSYPIK 227
Cdd:PRK06018 197 YSHRSNVLHALManNGDALGTSAADTMLPVvplfHANSWGIAFSAPSM-----GT-KLVMPGAKLDGASVYELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 228 SMMGAPIVYRMLLQQ-DLSSYKFPHLqNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK----------- 295
Cdd:PRK06018 271 FTAGVPTVWLMLLQYmEKEGLKLPHL-KMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAAlkppfsklpgd 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 296 ---TMKIKPGYmgtAASCYDVQIIDDKGNVLPpgTEGDIGIRVKpIRPIGIFSGYVdnpdKTAANIRGD--FWLLGDRGI 370
Cdd:PRK06018 350 arlDVLQKQGY---PPFGVEMKITDDAGKELP--WDGKTFGRLK-VRGPAVAAAYY----RVDGEILDDdgFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 371 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTK-ELQ 449
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG------ETATReEIL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 815659680 450 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD--KEWKMSGKA 495
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREqfKDYKLPTAA 541
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
133-486 |
5.92e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 104.55 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 133 SQEASAIY--FTSGTSGLPK--MAEHSYSSLGLKA-----KMDAGWTGLQASDIMWTISdtgwILNILCSLMepwaLGAC 203
Cdd:cd05918 103 SSPSDAAYviFTSGSTGKPKgvVIEHRALSTSALAhgralGLTSESRVLQFASYTFDVS----ILEIFTTLA----AGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 204 TFVhlLPKFDPLVIL-KTLSSYPIKSMMGAPIVYRMLLQQDlssykFPHLQNCVTVGESLLPETLENWraQTGLDIRESY 282
Cdd:cd05918 175 LCI--PSEEDRLNDLaGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRVRLINAY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 283 GQTETGLTCMVSK-TMKIKPGYMGTAASCydVQIIDDKGN---VLPPGTEGDI---GirvkPIrpigIFSGYVDNPDKTA 355
Cdd:cd05918 246 GPAECTIAATVSPvVPSTDPRNIGRPLGA--TCWVVDPDNhdrLVPIGAVGELlieG----PI----LARGYLNDPEKTA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 356 AN-IRGDFWLL-------------GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAV---VETAVISSP 418
Cdd:cd05918 316 AAfIEDPAWLKqegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGakeVVVEVVKPK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 419 DPVRGEVVKAFVVLASQFLSHDPEQ------------LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05918 396 DGSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
2-486 |
1.49e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 103.63 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLsGACGLQRGDRVAVVL---PRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyRLQMSKAKAI 78
Cdd:PRK07008 40 YTYRDCERRAKQLAQAL-AALGVEPGDRVGTLAwngYRHLEAYYGVSGSGAVCHTINP------------RLFPEQIAYI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 V--AGDEVI-------QEVDTVASECPSLRIKLLVSEKS---CDG--WLNFKKLLNEASTTHHCVETGSQEASAIYFTSG 144
Cdd:PRK07008 107 VnhAEDRYVlfdltflPLVDALAPQCPNVKGWVAMTDAAhlpAGStpLLCYETLVGAQDGDYDWPRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 145 TSGLPKMAEHSYSSLGLKAKM----DAgwTGLQASDI------MWTISdtGWILNILCslmepwALGACTFVHLLPKFDP 214
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGaalpDA--MGLSARDAvlpvvpMFHVN--AWGLPYSA------PLTGAKLVLPGPDLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 215 LVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLT 290
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 291 C-MVSKTMKIKPG-------YMGTAASCYDVQIIDDKGNVLP--PGTEGDIGIRvkpirpiG--IFSGYVdnpdKTAANI 358
Cdd:PRK07008 337 CkLKWKHSQLPLDeqrklleKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVR-------GpwVIDRYF----RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFl 437
Cdd:PRK07008 406 LVDGWFpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA- 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 815659680 438 shdpeQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK07008 485 -----EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
4-484 |
1.66e-23 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 102.77 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 83
Cdd:cd17643 15 YGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVP-------IDPAY--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevdtvasecPSLRIKLLV--SEKSCdgwlnfkkLLNEASTThhcvetgsqeASAIYfTSGTSGLPK--MAEHSySSL 159
Cdd:cd17643 72 ------------PVERIAFILadSGPSL--------LLTDPDDL----------AYVIY-TSGSTGRPKgvVVSHA-NVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAgWTGLQASDIMWTISDTGWILnilcSLMEPW-ALGACTFVHLLPKF---DPLVILKTLSSYPIKSMMGAPIV 235
Cdd:cd17643 120 ALFAATQR-WFGFNEDDVWTLFHSYAFDF----SVWEIWgALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQQDLSSYKFPH-LQNCVTVGESLLPETLENWRAQTGL---DIRESYGQTETglTCMVSKTmKIKPGYMGTAA--- 308
Cdd:cd17643 195 FYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET--TVHVTFR-PLDAADLPAAAasp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 -----SCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAANIRGD-FWLLGDRGIKDED-------G 375
Cdd:cd17643 272 igrplPGLRVYVLDADGRPVPPGVVGELYVS----GA-GVARGYLGRPELTAERFVANpFGGPGSRMYRTGDlarrlpdG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdPEQLTKELQQHVKSV 455
Cdd:cd17643 347 ELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAELRALLKEL 421
|
490 500
....*....|....*....|....*....
gi 815659680 456 TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17643 422 LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
4-481 |
2.12e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 102.91 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 83
Cdd:cd05914 10 YKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSSLglKA 163
Cdd:cd05914 89 -----DDVA---------------------------------------------LINYTSGTTGNSKGVMLTYRNI--VS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAG--WTGLQASDIMWTISDTGWILNILCSLMEPWALGActFVHLLPKFDPLVILKtLSSYPIKSMMGAPIVYRM--- 238
Cdd:cd05914 117 NVDGVkeVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGA--HVVFLDKIPSAKIIA-LAFAQVTPTLGVPVPLVIeki 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 239 -----LLQQDLSSYKFP------------------------HLQNCVTVGESLLPETLENWRaQTGLDIRESYGQTETGL 289
Cdd:cd05914 194 fkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGYGMTETAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 290 TCMVSKTMKIKPGYMGTAASCYDVQIIDDKgnvlPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDR 368
Cdd:cd05914 273 IISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDKDGWFhTGDL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 369 GIKDEDGYFQFMGRA-NDIINSSGYRIGPSEVENALMEHPAVVETAVIsspdpVRGEVVKAFVVLASQFL-------SHD 440
Cdd:cd05914 344 GKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvkalkqRNI 418
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 815659680 441 PEQLTKELQQHVKSVTAPYKYPRKIEFVL-NLPKTVTGKIQR 481
Cdd:cd05914 419 IDAIKWEVRDKVNQKVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
139-489 |
2.20e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.18 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWtisdtgwilniLC-------SLMEPW--ALGACTFVHLL 209
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCY-----------VSmplfhsnAVMAGWapAVASGAAVALP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 210 PKFDPLVILKTLSSYPIKSM--MGAPIVYRMLlqqdlSSYKFPHLQNCVTV--GESLLPETLENWRAQTGLDIRESYGQT 285
Cdd:PRK13388 224 AKFSASGFLDDVRRYGATYFnyVGKPLAYILA-----TPERPDDADNPLRVafGNEASPRDIAEFSRRFGCQVEDGYGSS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 286 ETGltCMVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGTEGDIGIRVKPIRPIG---------IFSGYVDNPDKTA 355
Cdd:PRK13388 299 EGA--VIVVREPGTPPGSIGRGAP--GVAIYNpETLTECAVARFDAHGALLNADEAIGelvntagagFFEGYYNNPEATA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 356 ANIR-GDFWLlGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAs 434
Cdd:PRK13388 375 ERMRhGMYWS-GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR- 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 435 QFLSHDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 489
Cdd:PRK13388 453 DGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
12-486 |
1.54e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 100.82 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 12 QQAANVLSG--ACGLQRGDRVAVVLPR----VPEWWlvilGCIRAGLIFMPGTIQMKSTDI------LYRL-QMSKAKAI 78
Cdd:cd05906 47 EDARRLAAGlrQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPnarlrkLRHIwQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 158
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIE-----------ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LgLKAKMDAGWT-GLQASDImwtisdtgwILNilcslmepWA----LGACTFVHLLPKF---------------DPLVIL 218
Cdd:cd05906 192 I-LARSAGKIQHnGLTPQDV---------FLN--------WVpldhVGGLVELHLRAVYlgcqqvhvpteeilaDPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIkSMMGAP-IVYRMLLQQ---------DLSSYKFphlqnCVTVGESLLPETLENWR---AQTGLD---IRESY 282
Cdd:cd05906 254 DLIDRYRV-TITWAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 283 GQTETGLTCMVSKTMkikPGYMGTAA-------SCY---DVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPD 352
Cdd:cd05906 328 GMTETCSGVIYSRSF---PTYDHSQAlefvslgRPIpgvSMRIVDDEGQLLPEGEVGRLQVRGPVV-----TKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 353 KTAANIRGDFWL-LGDRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVE--TAVISSPDPVRGEVVKAF 429
Cdd:cd05906 400 ANAEAFTEDGWFrTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815659680 430 VVLASQFLSHDPEQLTKELQQHVK---SVTAPYKYP-RKIEFvlnlPKTVTGKIQRAKLRD 486
Cdd:cd05906 479 FFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPlPKEEI----PKTSLGKIQRSKLKA 535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2-484 |
4.76e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 98.88 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 81
Cdd:cd12114 13 LTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 DEViqevdtvASECPSLRIKLLVSEKSCDGWLNFKKllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSySSL 159
Cdd:cd12114 92 GPD-------AQLDVAVFDVLILDLDALAAPAPPPP-----------VDVAPDDLAYVIFTSGSTGTPKgvMISHR-AAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWtGLQASDIMWTISDTGWILNILcSLMEPWALGAcTFVhlLP----KFDPLVILKTLSSYPIKSMMGAPIV 235
Cdd:cd12114 153 NTILDINRRF-AVGPDDRVLALSSLSFDLSVY-DIFGALSAGA-TLV--LPdearRRDPAHWAELIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRMLLQQDLSSYKFPHLQNCVTVGESL----LPETLenWRAQTGLDIRESYGQTETGLTCMVSKTMKIKP-------GYM 304
Cdd:cd12114 228 LEMLLDVLEAAQALLPSLRLVLLSGDWipldLPARL--RALAPDARLISLGGATEASIWSIYHPIDEVPPdwrsipyGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYdvqIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAA-----NIRGDFWLLGDRGIKDEDGYFQF 379
Cdd:cd12114 306 LANQRYR---VLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 380 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSvtapY 459
Cdd:cd12114 378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPA----Y 452
|
490 500
....*....|....*....|....*
gi 815659680 460 KYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd12114 453 MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
139-481 |
6.13e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 99.43 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSS--LGLKAKmdagWTGLQASD---IMWTISDTGWIL--NILCSLMepwALGaCTFVH---- 207
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPhlVGLKYY----WRSIIEKDiptVVFSHSSIGWVSfhGFLYGSL---SLG-NTFVMfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 208 -LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD------LSSYKFPHLQNCVTVGESL---LPETLENwraqtGLD 277
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIEN-----KLK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 278 IRES--YGQTETGLTCMVSKTMKIKPGY-MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVDNPD-- 352
Cdd:PTZ00237 406 IKSSrgYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkf 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 353 KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL 432
Cdd:PTZ00237 484 KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 815659680 433 ASQFLSH--DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 481
Cdd:PTZ00237 564 KQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
4-484 |
7.21e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 98.16 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 83
Cdd:cd12115 27 YAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqevdtvasecPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 161
Cdd:cd12115 84 ------------PPERLRFILEDAQA-----------------RLVLTDPDDLAYVIYTSGSTGRPKgvAIEHR----NA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 162 KAKMDagWTG-----------LQASDIMWTISdtgwILNILCSLMEpwalGACtfVHLLpkfDPLVILKTLSSYPIKSMM 230
Cdd:cd12115 131 AAFLQ--WAAaafsaeelagvLASTSICFDLS----VFELFGPLAT----GGK--VVLA---DNVLALPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GA-PIVYRMLLQQDlssyKFPHLQNCVTV-GESLLPETLENWRAQTGLD-IRESYGQTET---GLTCMVSKTMKIKPGyM 304
Cdd:cd12115 196 NTvPSAAAELLRHD----ALPASVRVVNLaGEPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEVS-I 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYF 377
Cdd:cd12115 271 GRPLANTQAYVLDRALQPVPLGVPGEL-----YIGGAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQHVKSVTA 457
Cdd:cd12115 346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV-----AEPGAAGLVEDLRRHLGTRLP 420
|
490 500
....*....|....*....|....*..
gi 815659680 458 PYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2-484 |
2.97e-21 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 96.08 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 81
Cdd:cd17645 24 LTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPK--MAEH-SYSS 158
Cdd:cd17645 101 -------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHhNLVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSlmepWALGACtfVHLLPKFDPLVILK----------TLSSYPIKs 228
Cdd:cd17645 132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPH----LTAGAA--LHVVPSERRLDLDAlndyfnqegiTISFLPTG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 229 mmgapiVYRMLLQQDLSSykfphLQNCVTVGESLlpetleNWRAQTGLDIRESYGQTEtgltCMVSKTM-KIKPGY---- 303
Cdd:cd17645 205 ------AAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYanip 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 304 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKD-------EDGY 376
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflPDGN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 377 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEqltkELQQHVKSVT 456
Cdd:cd17645 339 IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PHE----ELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 815659680 457 APYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-484 |
8.15e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDE 83
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLRIkllvsekSCDGWLNfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL---- 159
Cdd:PRK12316 2109 HLLERLPLPAGVARLPL-------DRDAEWA------DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALvahc 2175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 ---GLKAKMDAGWTGLQASDIMWTISDTGWilnilcslMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY 236
Cdd:PRK12316 2176 qaaGERYELSPADCELQFMSFSFDGAHEQW--------FHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYL 2247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 237 RMLLQQDLSSYKFPHLQNCVTVGESLLPETLEN-WRAQTGLDIRESYGQTETGLTCMVSKTMKIKPG---YM--GTAASC 310
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgaaYVpiGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 311 YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGR 382
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGR 2402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 383 ANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVlasqflSHDP-EQLTKELQQHVKSVTAPYKY 461
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV------PDDAaEDLLAELRAWLAARLPAYMV 2475
|
490 500
....*....|....*....|...
gi 815659680 462 PRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK12316 2476 PAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
139-484 |
1.68e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 94.29 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKmaehsysSLGLKAKMDAGwTGLQASDIMWTISDTGWILNI---------LCSLMEPWALGACTFVHll 209
Cdd:PRK13383 179 VLLTSGTTGKPK-------GVPRAPQLRSA-VGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 210 PKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE 286
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 287 TGLTCMVSKT-MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKtaANIRGdFWLL 365
Cdd:PRK13383 329 VGIGALATPAdLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG-----TRYTDGGGK--AVVDG-MTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 366 GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEQlt 445
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ-- 477
|
330 340 350
....*....|....*....|....*....|....*....
gi 815659680 446 keLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK13383 478 --LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-484 |
4.51e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.25 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 80
Cdd:PRK12316 539 YAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSqsh 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 -GDE--VIQEVDTVASECPSLrikllvsekscdgWLNFKKllNEASTTHHCVEtgsQEASAIYfTSGTSGLPKMAEHSYS 157
Cdd:PRK12316 618 lGRKlpLAAGVQVLDLDRPAA-------------WLEGYS--EENPGTELNPE---NLAYVIY-TSGSTGKPKGAGNRHR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLglKAKMDAGWT--GLQASDIMWTISDTGWILNILcslMEPWALGACTFVHLLPK---FDPLVILKTLSSYPIKSMMGA 232
Cdd:PRK12316 679 AL--SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVW---EFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFV 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 233 PIVYRMLLQ----QDLSSykfphLQNCVTVGESL---LPETLENWRAQTGLdiRESYGQTETGL-----TCMVSKTMKIK 300
Cdd:PRK12316 754 PSMLQAFLQdedvASCTS-----LRRIVCSGEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdvthwTCVEEGGDSVP 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 301 PGYMGTAASCYdvqIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTA----ANIRGD---FWLLGDRGIKDE 373
Cdd:PRK12316 827 IGRPIANLACY---ILDANLEPVPVGVLGELYLAGR-----GLARGYHGRPGLTAerfvPSPFVAgerMYRTGDLARYRA 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 374 DGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLasqflsHDPEQLTKE-LQQHV 452
Cdd:PRK12316 899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL------ESEGGDWREaLKAHL 968
|
490 500 510
....*....|....*....|....*....|..
gi 815659680 453 KSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK12316 969 AASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2-484 |
7.60e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 92.15 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 81
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 deviqevdtvasecpslrikLLVSEKSCDGWLNFKK--------LLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--M 151
Cdd:cd17656 88 --------------------VVLTQRHLKSKLSFNKstilledpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 152 AEHSySSLGL------KAKMDAGWTGLQASDIMWTISDTGwILNILCSlmepwalGACtfVHLLPK-----FDPLVILkt 220
Cdd:cd17656 148 LEHK-NMVNLlhfereKTNINFSDKVLQFATCSFDVCYQE-IFSTLLS-------GGT--LYIIREetkrdVEQLFDL-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 221 LSSYPIKSMmgapIVYRMLLQQDLSSYKF-PHLQNCV----TVGESL-LPETLENWRAQTGLDIRESYGQTETGL--TCM 292
Cdd:cd17656 215 VKRHNIEVV----FLPVAFLKFIFSEREFiNRFPTCVkhiiTAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVvtTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 293 VSKTMKIkPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA---------ANIRgd 361
Cdd:cd17656 291 INPEAEI-PELppIGKPISNTWIYILDQEQQLQPQGIVGEL-----YISGASVARGYLNRQELTAekffpdpfdPNER-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 362 FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflshdP 441
Cdd:cd17656 363 MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------M 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 815659680 442 EQL--TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17656 434 EQElnISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
2-486 |
7.61e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 92.30 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGACGlqRGDRVAVVLPRVPEWWLVILGCIRAGLI----FMPGtiqmkSTDILYRLQ----MS 73
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPPPT-----PGRHAERLAailaDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 74 KAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 153
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDL---------LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 154 HSYSSLG--LKAkMDAGWtGLQASDIM--W--TISDTGWILNIL--------CSLMEPWAlgactFVHllpkfDPLVILK 219
Cdd:cd05931 169 VTHRNLLanVRQ-IRRAY-GLDPGDVVvsWlpLYHDMGLIGGLLtplysggpSVLMSPAA-----FLR-----RPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 220 TLSSYPIkSMMGAP------IVYRMLLQQ----DLSSykfphLQNCVTVGESLLPETLENWR---AQTGLD---IRESYG 283
Cdd:cd05931 237 LISRYRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRPATLRRFAeafAPFGFRpeaFRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 284 QTETglTCMVSkTMKIKPGY-----------------------------MGTAASCYDVQIIDDKGN-VLPPGTEGDIGI 333
Cdd:cd05931 311 LAEA--TLFVS-GGPPGTGPvvlrvdrdalagravavaaddpaarelvsCGRPLPDQEVRIVDPETGrELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 334 RvkpirpiG--IFSGYVDNPDKTA------ANIRGDFWL-LGDRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALM 404
Cdd:cd05931 388 R-------GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 405 E-HPAVVET--AVISSPDPVRGEVVkAFVVLASQFLSHDPEQLTKELQQHVKS---VTapykyPRKIEFVLN--LPKTVT 476
Cdd:cd05931 460 EaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRPgsIPRTSS 533
|
570
....*....|
gi 815659680 477 GKIQRAKLRD 486
Cdd:cd05931 534 GKIQRRACRA 543
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-484 |
8.31e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 129 VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILcSLMEPWALGACTFVHL 208
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLAG 3269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 209 LPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTET 287
Cdd:PRK12316 3270 PEDWrDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 288 GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGDFWLL 365
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGEL-----YLGGEGLARGYHNRPGLTAERFVPDPFVP 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 366 GDRGIKD-------EDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQfls 438
Cdd:PRK12316 3422 GERLYRTgdlaryrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE--- 3494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 815659680 439 hdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK12316 3495 --AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
45-484 |
2.50e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 90.72 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 45 LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEAST 124
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 125 THhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdimwtISDTGWILN---------IL---- 191
Cdd:PRK04813 146 YY------------IIFTSGTTGKPKGVQISHDNL---------------------VSFTNWMLEdfalpegpqFLnqap 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 192 ----CSLMEpW----ALGAcTFVhLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRM-LLQQDLSSYKFPHLQNCVTVG 259
Cdd:PRK04813 193 ysfdLSVMD-LyptlASGG-TLV-ALPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 260 ESLLPETlenwrAQTGLD------IRESYGQTETglTCMVSK---TMKIKPGY----MGTAASCYDVQIIDDKGNVLPPG 326
Cdd:PRK04813 270 EELPHKT-----AKKLLErfpsatIYNTYGPTEA--TVAVTSieiTDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPDG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 327 TEGDIGIrvkpirpIG--IFSGYVDNPDKTAANirgdFWLL--------GDRGIKDeDGYFQFMGRANDIINSSGYRIGP 396
Cdd:PRK04813 343 EQGEIVI-------SGpsVSKGYLNNPEKTAEA----FFTFdgqpayhtGDAGYLE-DGLLFYQGRIDFQIKLNGYRIEL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 397 SEVENALMEHPAVVETAVIsspdPV-RGEVVK---AFVVLASqflsHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVL 469
Cdd:PRK04813 411 EEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRD 482
|
490
....*....|....*
gi 815659680 470 NLPKTVTGKIQRAKL 484
Cdd:PRK04813 483 SLPLTPNGKIDRKAL 497
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
128-486 |
4.93e-19 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 89.70 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 128 CVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDAgwtglQASDIMwtisdtgwiLNIL---------CS 193
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP-----NPEDVV---------FGALpffhsfgltGC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 194 LMEPWALGACTFVHllpkFDPL---VILKTLSSYPIKSMMGAPIVYRMLLQQdLSSYKFPHLQNCVTVGESLLPETLENW 270
Cdd:cd05909 207 LWLPLLSGIKVVFH----PNPLdykKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 271 RAQTGLDIRESYGQTETGLTCMVSK-TMKIKPGYMGTAASCYDVQIIDDKGNV-LPPGTEGDIGIRvkpirpiG--IFSG 346
Cdd:cd05909 282 QEKFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-------GpnVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 347 YVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEH-PAVVETAVISSPDPVRGEV 425
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815659680 426 VKAFVVLasqflsHDPEQLtkELQQHVKSVTAPYKY-PRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:cd05909 435 IVLLTTT------TDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
4-484 |
5.36e-19 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 89.38 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRvPEWWLV-ILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagd 82
Cdd:cd17648 15 YRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP-------IDPSY-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 eviqevdtvasecPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSySSLG 160
Cdd:cd17648 73 -------------PDERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHG-SVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 LKAKMDAGWtGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP--KFDPLVILKTLSSYPIKSMMGAPIVyrm 238
Cdd:cd17648 122 LRTSLSERY-FGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDemRFDPDRFYAYINREKVTYLSGTPSV--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 239 lLQQ-DLSSykFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-------KTMKIKPGYMGTAasC 310
Cdd:cd17648 198 -LQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRffpgdqrFDKSLGRPVRNTK--C 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 311 YdvqIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----AN--------IRGDFWLL---GDRGIKDEDG 375
Cdd:cd17648 273 Y---VLNDAMKRVPVGAVGEL-----YLGGDGVARGYLNRPELTAerflPNpfqteqerARGRNARLyktGDLVRWLPSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 376 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRG-EVVKAFVVlasQFLSHDPEQLTK-ELQQHVK 453
Cdd:cd17648 345 ELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqSRIQKYLV---GYYLPEPGHVPEsDLLSFLR 421
|
490 500 510
....*....|....*....|....*....|.
gi 815659680 454 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17648 422 AKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
4-484 |
2.17e-18 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 88.12 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEW---W--LVILGCIRAgliFMPGTIQMKStdILYRLQMSKAKAI 78
Cdd:cd05938 8 YRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCPVA---FLNTNIRSKS--LLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEVIQEVDTVaseCPSLR-----IKLLVSEKSCDGWLNFKKLLNEASTT-----HHCVETGSQEASAIYfTSGTSGL 148
Cdd:cd05938 83 VVAPELQEAVEEV---LPALRadgvsVWYLSHTSNTEGVISLLDKVDAASDEpvpasLRAHVTIKSPALYIY-TSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 149 PKMAEHSYsslgLKAKMDAGWT---GLQASDIMWTI----SDTGWILNILCSLmepwALGAcTFVhLLPKFDPLVILKTL 221
Cdd:cd05938 159 PKAARISH----LRVLQCSGFLslcGVTADDVIYITlplyHSSGFLLGIGGCI----ELGA-TCV-LKPKFSASQFWDDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 222 SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTG-LDIRESYGQTEtGLTCMVSKTMKIk 300
Cdd:cd05938 229 RKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVR-LAIGNGLRADVWREFLRRFGpIRIREFYGSTE-GNIGFFNYTGKI- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 301 pGYMGTaASC------------YDVQ----IIDDKGNVLPPGTeGDIGIRVKPIRPIGIFSGYVDNP----DKTAANI-- 358
Cdd:cd05938 306 -GAVGR-VSYlykllfpfelikFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKeqteKKLLRDVfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLAsqf 436
Cdd:cd05938 383 KGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLK--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 815659680 437 lshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd05938 460 ---PGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-414 |
3.25e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 87.62 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIF-MPGTIQMKstDIL-YRLQMSKAKAIV 79
Cdd:PRK08279 63 ISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVVaLLNTQQRG--AVLaHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVASECPSLRIKLLVSEKSCD---GWLNFKKLLNEASTTHHCVETGSQ-EASAIY-FTSGTSGLPKMAEH 154
Cdd:PRK08279 140 VGEELVEAFEEARADLARPPRLWVAGGDTLDdpeGYEDLAAAAAGAPTTNPASRSGVTaKDTAFYiYTSGTTGLPKAAVM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 155 SYSSLGLKAKMDAGWTGLQASDIMWTI----SDTGwiLNI-LCSLMepwaLGACTFVhLLPKFD-----PLVILK--TLs 222
Cdd:PRK08279 220 SHMRWLKAMGGFGGLLRLTPDDVLYCClplyHNTG--GTVaWSSVL----AAGATLA-LRRKFSasrfwDDVRRYraTA- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 223 sypiksmmgapIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLPETLENWRAQTGLD-IRESYGQTE--TGLTCM-- 292
Cdd:PRK08279 292 -----------FQYigelcRYLLNQPPKPTDRDHRLRLM-IGNGLRPDIWDEFQQRFGIPrILEFYAASEgnVGFINVfn 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 293 VSKTMKIKPGYMGTAASC--YDVQ----IIDDKGNVLPPGTeGDIGIRVKPIRPIGIFSGYVDnPDKTAANI------RG 360
Cdd:PRK08279 360 FDGTVGRVPLWLAHPYAIvkYDVDtgepVRDADGRCIKVKP-GEVGLLIGRITDRGPFDGYTD-PEASEKKIlrdvfkKG 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 361 DFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAV 414
Cdd:PRK08279 438 DAWFnTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV 492
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
21-484 |
7.45e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.22 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 21 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQEVDTVASECPS 97
Cdd:PRK05857 60 AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 98 LRIKLL--VSEKSCDGWLNFKKLLneastthhcVETGSQEASAIYFTSGTSGLPK---MAEHSYSSLG--LKAK------ 164
Cdd:PRK05857 140 IAVDIAavTRESEHSLDAASLAGN---------ADQGSEDPLAMIFTSGTTGEPKavlLANRTFFAVPdiLQKEglnwvt 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 165 ---MDAGWTGLQASDI--MWtisdtgWILNilcSLMEPwalGACtfvhLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM 238
Cdd:PRK05857 211 wvvGETTYSPLPATHIggLW------WILT---CLMHG---GLC----VTGGENTTSLLEILTTNAVATTCLVPtLLSKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 239 LLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKT-----MKIKPGYMGTAASCYDV 313
Cdd:PRK05857 275 VSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 314 QIID-DKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAaNIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSG 391
Cdd:PRK05857 354 YLAAtDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTA-EVLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 392 YRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNL 471
Cdd:PRK05857 433 VNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDI 512
|
490
....*....|...
gi 815659680 472 PKTVTGKIQRAKL 484
Cdd:PRK05857 513 PRTQSGKVMRASL 525
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
2-485 |
1.39e-17 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 85.17 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 81
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 82 dEVIQEVDTVASECPslrikllvseKSCDGwLNFKKLLneastthhcvetgsqeaSAIYfTSGTSGLPKMA--EHS--YS 157
Cdd:cd05939 82 -NLLDPLLTQSSTEP----------PSQDD-VNFRDKL-----------------FYIY-TSGTTGLPKAAviVHSryYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLGLKAKMdagwTGLQASDIMWT----ISDTGWILNILCSLmepwaLGACTFVhLLPKFDPLVILKTLSSY--PIKSMMG 231
Cdd:cd05939 132 IAAGAYYA----FGMRPEDVVYDclplYHSAGGIMGVGQAL-----LHGSTVV-IRKKFSASNFWDDCVKYncTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 232 ApiVYRMLLQQDLSSYKFPHlqnCV--TVGESLLPETLENWRAQTGL-DIRESYGQTEtGLTCMVSKTMKIKP-GYMG-T 306
Cdd:cd05939 202 E--ICRYLLAQPPSEEEQKH---NVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATE-GNSSLVNIDNHVGAcGFNSrI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 307 AASCYDVQII-----------DDKGNVLP--PGTEGDIGIRVKPIRPIGIFSGYVDNPD---KTAANI--RGD-FWLLGD 367
Cdd:cd05939 276 LPSVYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGAtnkKIARDVfkKGDsAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 368 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQFLshDPEQLTK 446
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPERKV--DLDRFSA 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 815659680 447 ELQqhvkSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05939 434 VLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
2-489 |
1.40e-17 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 85.18 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTIQ--MKSTDILYRLQMSKAKAIV 79
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEViqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqEASAIYfTSGTSGLPKMAEHSYSSL 159
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAAAISWRRT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDAGWTGLQASDIMWT----ISDTGWILNILCSLMEpwalGACtfVHLLPKFDplviLKTLSSYPIKSmmGAP-I 234
Cdd:cd05937 113 LVTSNLLSHDLNLKNGDRTYTcmplYHGTAAFLGACNCLMS----GGT--LALSRKFS----ASQFWKDVRDS--GATiI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 235 VY-----RMLLQQDLSSYKFPHLQNCVTvGESLLPETLENWRAQTGL-DIRESYGQTETgltcmVSKTMKIKPGYMGTAA 308
Cdd:cd05937 181 QYvgelcRYLLSTPPSPYDRDHKVRVAW-GNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNVGDFGAGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 309 SCYD--------------VQIIDDKGNVL-----------PPGTEGDIGIRVkPIRPIGIFSGYVDNPDKTAANI----- 358
Cdd:cd05937 255 IGHHglirrwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrdvf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 -RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQ 435
Cdd:cd05937 334 rKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 436 flSHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 489
Cdd:cd05937 414 --SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
264-486 |
2.46e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 84.28 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 264 PETLENWRaQTGLDIRESYGQTETGltcmvSKTMKIKPG-YMGTAASCydvqiiddkGNVLPPGTegdIGIRVKPIRPIG 342
Cdd:PRK07445 244 PSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKPDdFLAGNNSS---------GQVLPHAQ---ITIPANQTGNIT 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 343 I-----FSGYVdnPDKTAANIrgdFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISS 417
Cdd:PRK07445 306 IqaqslALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815659680 418 PDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK07445 381 PDPHWGEVVTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
233-484 |
1.02e-16 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 82.48 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 233 PIVYRMLLQQDLSSYKFP---HLQNCVTVGESLLPETLENWRAQTGLDIR--ESYGQTETGLTCMVS-----KTMKIKPG 302
Cdd:cd17644 204 PPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEATIAATVCrltqlTERNITSV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 303 YMGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD---------FWLLGDRGIKDE 373
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGEL-----HIGGVGLARGYLNRPELTAEKFISHpfnsseserLYKTGDLARYLP 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 374 DGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQ-LTKELQQHV 452
Cdd:cd17644 359 DGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV------PHYEESpSTVELRQFL 432
|
250 260 270
....*....|....*....|....*....|..
gi 815659680 453 KSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17644 433 KAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
3-453 |
1.13e-16 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 82.41 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagd 82
Cdd:cd17640 7 TYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 eviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSysslG 160
Cdd:cd17640 83 ----------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTHA----N 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 161 LKAKMDAGWTGLQAS--DIMWTISDTGWILNILCSLMEPWALGACTF---VHL---LPKFDPLVIL------KTLSSYPI 226
Cdd:cd17640 113 LLHQIRSLSDIVPPQpgDRFLSILPIWHSYERSAEYFIFACGCSQAYtsiRTLkddLKRVKPHYIVsvprlwESLYSGIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 227 KSMMGAPIVYRMLLQQDLS--SYKFPhlqncVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYM 304
Cdd:cd17640 193 KQVSKSSPIKQFLFLFFLSggIFKFG-----ISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 305 GTAASCYDVQIIDDKGN-VLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 382
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLGWLTCGGELVLTGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 383 AND-IINSSGYRIGPSEVENALMEHPaVVETAVISSPD---------PVRGEVVKAFVVLAsQFLSHDPEQL------TK 446
Cdd:cd17640 342 AKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMVVGQDqkrlgalivPNFEELEKWAKESG-VKLANDRSQLlaskkvLK 419
|
....*..
gi 815659680 447 ELQQHVK 453
Cdd:cd17640 420 LYKNEIK 426
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
6-487 |
3.68e-16 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 81.28 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 6 ELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKA------IV 79
Cdd:PLN03052 213 ELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAiftqdvIV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AGDEVIQEVDTVASECPSLRIKLLVSEKSC-----DGWLNFKKLLNEASTTHHCVETGSQEASA-----IYFTSGTSGLP 149
Cdd:PLN03052 292 RGGKSIPLYSRVVEAKAPKAIVLPADGKSVrvklrEGDMSWDDFLARANGLRRPDEYKAVEQPVeaftnILFSSGTTGEP 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 150 KMAEHSYSSlGLKAKMDAgWTGL--QASDIMWTISDTGWilnilcsLMEPWALGACtfvhllpkfdpLVILKTLSSY--- 224
Cdd:PLN03052 372 KAIPWTQLT-PLRAAADA-WAHLdiRKGDIVCWPTNLGW-------MMGPWLVYAS-----------LLNGATLALYngs 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 225 PIKS------------MMGA--PIVYRMLLQQDLSSYKFPHLQNCVTVGE-SLLPETLenW---RAQTGlDIRESYGQTE 286
Cdd:PLN03052 432 PLGRgfakfvqdakvtMLGTvpSIVKTWKNTNCMAGLDWSSIRCFGSTGEaSSVDDYL--WlmsRAGYK-PIIEYCGGTE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 287 TGlTCMVSKTMkIKP---GYMGTAASCYDVQIIDDKGNVLP---PGTeGDIGIRVKpirpigIF--SGYVDNPDKTAANI 358
Cdd:PLN03052 509 LG-GGFVTGSL-LQPqafAAFSTPAMGCKLFILDDSGNPYPddaPCT-GELALFPL------MFgaSSTLLNADHYKVYF 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 359 RG-DFW---LL---GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVE---NALmeHPAVVETAVISSPDPVRG--EVV 426
Cdd:PLN03052 580 KGmPVFngkILrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcNAA--DESVLETAAIGVPPPGGGpeQLV 657
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815659680 427 KAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 487
Cdd:PLN03052 658 IAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1-484 |
5.57e-16 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 80.20 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 1 MWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVa 80
Cdd:cd17650 12 QLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 gdevIQEVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPK--MAEHSYSs 158
Cdd:cd17650 90 ----TQPEDL---------------------------------------------AYVIY-TSGTTGKPKgvMVEHRNV- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 lglkAKMDAGW-----------TGLQASDIMWTISdTGWILNILCslmepwALGACTFVHLLPKFDPLVILKTLSSYPIK 227
Cdd:cd17650 119 ----AHAAHAWrreyeldsfpvRLLQMASFSFDVF-AGDFARSLL------NGGTLVICPDEVKLDPAALYDLILKSRIT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 228 SMMGAPIVYRMLL------QQDLSSYKFphlqncVTVGESLLPETLENW---RAQTGLDIRESYGQTETgltCMVSKTMK 298
Cdd:cd17650 188 LMESTPALIRPVMayvyrnGLDLSAMRL------LIVGSDGCKAQDFKTlaaRFGQGMRIINSYGVTEA---TIDSTYYE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 299 IKPGYMGTAASC--------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD-------FW 363
Cdd:cd17650 259 EGRDPLGDSANVpigrplpnTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapgerMY 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 364 LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLShdpeq 443
Cdd:cd17650 334 RTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLCAYVVAAATLN----- 407
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 815659680 444 lTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17650 408 -TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
3-451 |
8.82e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 79.94 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFM---PGtiqMKSTDILYRLQMSKAKAIV 79
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 AgdeviQEVDTVAS-----ECPSLRIKLLVSEKSCDGWLNFKKLlnEASTTHH---CVETGSQEASAIYFTSGTSGLPKM 151
Cdd:PRK09274 119 G-----IPKAHLARrlfgwGKPSVRRLVTVGGRLLWGGTTLATL--LRDGAAApfpMADLAPDDMAAILFTSGSTGTPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 152 AEHSYSSLglkakmDAGWTGLQASdimWTISDTGWILNI--LCSLMEPwALGACTfvhLLPKFD--------PLVILKTL 221
Cdd:PRK09274 192 VVYTHGMF------EAQIEALRED---YGIEPGEIDLPTfpLFALFGP-ALGMTS---VIPDMDptrpatvdPAKLFAAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 222 SSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRA--QTGLDIRESYGQTETGLTCMVS---- 294
Cdd:PRK09274 259 ERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPISSIEsrei 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 295 --KTMKIK---PGY-MGTAASCYDVQIID---------DKGNVLPPGTEGDIgirvkpirpigIFSG------YVDNPDK 353
Cdd:PRK09274 339 lfATRAATdngAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI-----------VVAGpmvtrsYYNRPEA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 354 TAAN----IRGDFW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvrGEVVKA 428
Cdd:PRK09274 408 TRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPV 485
|
490 500
....*....|....*....|...
gi 815659680 429 FVVLASQFLSHDPEQLTKELQQH 451
Cdd:PRK09274 486 LCVELEPGVACSKSALYQELRAL 508
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
2-485 |
6.13e-15 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 77.01 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTI--QMKSTDILYRLQMSKAKAIV 79
Cdd:cd05940 4 LTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 80 agdeviqeVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIY-FTSGTSGLPKMAEHSYSS 158
Cdd:cd05940 81 --------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 159 LGLKAKMDAGWTGLQASDIMWTI----SDTGWILNILCSLMEpwalGACtfvhllpkfdpLVILKTLSSY----PIKSMM 230
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYTClplyHSTALIVGWSACLAS----GAT-----------LVIRKKFSASnfwdDIRKYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLPETLENWRAQTGL-DIRESYGQTE--------TGLTCMVSKT 296
Cdd:cd05940 171 ATIFQYigelcRYLLNQPPKPTERKHKVRMI-FGNGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinfFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 297 MKIKPGYMGTAASCYDVQ----IIDDKGNVLPPGtEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIR-----GDFWLL-G 366
Cdd:cd05940 250 PSLLRKVAPLALVKYDLEsgepIRDAEGRCIKVP-RGEPGLLISRINPLEPFDGYTDPAATEKKILRdvfkkGDAWFNtG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 367 DRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQflshDPEQLT 445
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN----EEFDLS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 815659680 446 KeLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:cd05940 405 A-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
139-493 |
2.81e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 139 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---IMWTISDTGWILNILCSLMEpwalGACTFVHLLPKFDPL 215
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDrvlLFMSFSFDGAQERFLWTLIC----GGCLVVRDNDLWDPE 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 216 VILKTLSSYPIkSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRA---QTGLdiRESYGQTETGLTCM 292
Cdd:PRK12467 3318 ELWQAIHAHRI-SIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRklkPRGL--TNGYGPTEAVVTVT 3394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 293 VSKTmkIKPGYMGTAA----------SCYdvqIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD- 361
Cdd:PRK12467 3395 LWKC--GGDAVCEAPYapigrpvagrSIY---VLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAERFVADp 3464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 362 FWLLGDRGIKD-------EDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLas 434
Cdd:PRK12467 3465 FSGSGGRLYRTgdlaryrADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP-- 3541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 435 qflsHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSG 493
Cdd:PRK12467 3542 ----ADPQGdWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
5-483 |
3.34e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.03 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 5 RELSENSQQAANVLSGAcGLQRGDRVAV-------VLPRVPEWWLvilgciRAGLIFM-----PGT-IQMKSTDILYRLQ 71
Cdd:PRK07768 33 GEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLWM------RGASLTMlhqptPRTdLAVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 72 MSKAKAIVAGDEVIQEVDTVASEcpSLRIkLLVSEkscdgwlnfkkLLNEASTTHhcVETGsQEASAIY-FTSGTSGLPK 150
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK--GIRV-LTVAD-----------LLAADPIDP--VETG-EDDLALMqLTSGSTGSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 MAEHSYSSLglKAKMDAGWTGLQA---SDIM--W--TISDTGWIlNILCSlmePWALGaCTFVHLLP-KF--DPLVILKT 220
Cdd:PRK07768 169 AVQITHGNL--YANAEAMFVAAEFdveTDVMvsWlpLFHDMGMV-GFLTV---PMYFG-AELVKVTPmDFlrDPLLWAEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 221 LSSYPiKSMMGAP-----IVYRMLLQQ------DLSSYKFphlqnCVTVGESLLPETLENWRAQT---GLD---IRESYG 283
Cdd:PRK07768 242 ISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLLDAGarfGLRpeaILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 284 QTETGLTC-----------------MVSKTMKIKPGYMGTAASC---------YDVQIIDDKGNVLPPGTEGDIGIRVKP 337
Cdd:PRK07768 316 MAEATLAVsfspcgaglvvdevdadLLAALRRAVPATKGNTRRLatlgpplpgLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 338 IRPigifsGYVDnPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIS 416
Cdd:PRK07768 396 VTP-----GYLT-MDGFIPAQDADGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815659680 417 SPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY-PRKIeFVL---NLPKTVTGKIQRAK 483
Cdd:PRK07768 470 VRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKLRRAN 538
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-484 |
6.43e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 74.70 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKA 75
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP-------LDTGYpddRLKMmledARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 76 KAIVAGDEVIQE-VDTVASECPSLRIKLLVSEKSCDGwlnfkkllneASTTHHcvetgsqeASAIYFTSGTSGLPK--MA 152
Cdd:PRK10252 557 SLLITTADQLPRfADVPDLTSLCYNAPLAPQGAAPLQ----------LSQPHH--------TAYIIFTSGSTGRPKgvMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 153 EHsysslglkakmdagwtglQAsdimwtisdtgwILNILCSLMEPWALGA---------CTF-VHLLPKF---------- 212
Cdd:PRK10252 619 GQ------------------TA------------IVNRLLWMQNHYPLTAddvvlqktpCSFdVSVWEFFwpfiagaklv 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 --------DPLVILKTLSSYPIKSMMGAPivyRML------LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDI 278
Cdd:PRK10252 669 maepeahrDPLAMQQFFAEYGVTTTHFVP---SMLaafvasLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 279 RESYGQTETG------------LTCMVSKTMKIKPGYMGTAascydVQIIDDKGNVLPPGTEGDI---GIRVKpirpigi 343
Cdd:PRK10252 746 HNLYGPTEAAvdvswypafgeeLAAVRGSSVPIGYPVWNTG-----LRILDARMRPVPPGVAGDLyltGIQLA------- 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 344 fSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHP----AVVET 412
Cdd:PRK10252 814 -QGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHA 892
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815659680 413 AVISSPDPVRGEVVK--AFVVlASQFLSHDpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK10252 893 CVINQAAATGGDARQlvGYLV-SQSGLPLD----TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
367-485 |
7.46e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.77 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 367 DRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHDPEQLTK 446
Cdd:PRK07824 240 DLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD-----GGPAPTLE 313
|
90 100 110
....*....|....*....|....*....|....*....
gi 815659680 447 ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
255-484 |
1.39e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 255 CVTVGESLLPETLENWRA--QTGLdIRESYGQTET---GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGT 327
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQafAPQL-FFNAYGPTETvvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGA 2531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 328 EGDIGIRVKpirpiGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEV 399
Cdd:PRK05691 2532 TGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEI 2606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 400 ENALMEHPAVVETAVISSPDPVRGEVVKafvVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVT 476
Cdd:PRK05691 2607 ESRLLEHPAVREAVVLALDTPSGKQLAG---YLVSAVAGQDDEAqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTAN 2683
|
....*...
gi 815659680 477 GKIQRAKL 484
Cdd:PRK05691 2684 GKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-490 |
6.45e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 3 NFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 82
Cdd:PRK05691 1158 DYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 83 EVIQEVDTVASECPslrikLLVSEKSCDGWLNFKKLLNeastTHhcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGLK 162
Cdd:PRK05691 1237 HLLERLPQAEGVSA-----IALDSLHLDSWPSQAPGLH----LH-----GDNLAYVIY-TSGSTGQPKGVGNTHAALAER 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 163 AK-MDAGWtGLQASDIMWTISDTGWILNIL-CSlmepWAL-GACTFVHLLP--KFDPLVILKTLSSYPIKSMMGAPIVYR 237
Cdd:PRK05691 1302 LQwMQATY-ALDDSDVLMQKAPISFDVSVWeCF----WPLiTGCRLVLAGPgeHRDPQRIAELVQQYGVTTLHFVPPLLQ 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 238 MLLQQdlssykfPHLQNCVTV------GESLLPETLENWRAQ-TGLDIRESYGQTETGLT-----CMVSKTMKIKPGYMG 305
Cdd:PRK05691 1377 LFIDE-------PLAAACTSLrrlfsgGEALPAELRNRVLQRlPQVQLHNRYGPTETAINvthwqCQAEDGERSPIGRPL 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 306 TAASCydvQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYF 377
Cdd:PRK05691 1450 GNVLC---RVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAERFVPDplgedgarLYRTGDRARWNADGAL 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 378 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKELQQHVKSVTA 457
Cdd:PRK05691 1522 EYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQ------EAEAERLKAALAAELP 1595
|
490 500 510
....*....|....*....|....*....|...
gi 815659680 458 PYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 490
Cdd:PRK05691 1596 EYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ 1628
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-484 |
1.20e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP---GTIQMKSTDILyrlQMSKAKAI 78
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRTPVL 3821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 VAGDEVIQEVDTVASECP-SLRIKLLVSEKscdgwlnfkkLLNEASTTHH-CVETGSQEASAIYFTSGTSGLPK------ 150
Cdd:PRK05691 3822 VCSAACREQARALLDELGcANRPRLLVWEE----------VQAGEVASHNpGIYSGPDNLAYVIYTSGSTGLPKgvmveq 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 --MAEHSYSS---LGLKAKMDAGWTGLQASDI-MWTIsdtgwilnilcslmepwaLGACTF---VHLLPK---FDPLVIL 218
Cdd:PRK05691 3892 rgMLNNQLSKvpyLALSEADVIAQTASQSFDIsVWQF------------------LAAPLFgarVEIVPNaiaHDPQGLL 3953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 219 KTLSSYPIKSMMGAP-IVYRMLLQQDLSsykFPHLQNCVTVGESLLPETLENW---RAQTGLdiRESYGQTEtgltC--- 291
Cdd:PRK05691 3954 AHVQAQGITVLESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWlqrYPQIGL--VNAYGPAE----Csdd 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 292 -------MVSKTMKIKPgyMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTA----ANIRG 360
Cdd:PRK05691 4025 vaffrvdLASTRGSYLP--IGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFG 4097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 361 D----FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLASQF 436
Cdd:PRK05691 4098 ApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTV 4176
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 815659680 437 lsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:PRK05691 4177 --LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
304-485 |
1.19e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.74 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 304 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLL-GDRG-IKDEDGYFqfMG 381
Cdd:cd05908 316 VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLVI--TG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 382 RANDIINSSGYRIGPSEVENalmehpavvetaVISSPDPVR-GEVVKAFVvlasqflsHDPEQLTKEL---QQHVKSVTA 457
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIER------------IAEELEGVElGRVVACGV--------NNSNTRNEEIfcfIEHRKSEDD 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 815659680 458 PYKYPRKIEFVLN---------------LPKTVTGKIQRAKLR 485
Cdd:cd05908 449 FYPLGKKIKKHLNkrggwqinevlpirrIPKTTSGKVKRYELA 491
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
21-480 |
7.70e-11 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 64.60 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 21 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTV 91
Cdd:cd05943 117 ALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrEKVAEL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 92 ASECPSLRIKLLVSEKSCDGWLNFKKLLNeastTHHCVETGSQEASA--------------IYFTSGTSGLPKMAEHSYS 157
Cdd:cd05943 197 VKGLPSLLAVVVVPYTVAAGQPDLSKIAK----ALTLEDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 158 SLGLKAKMDAGW-TGLQASDIMWTISDTGWIL-NILCSLMepwALGAcTFV-----HLLPkfDPLVILKTLSSYPIkSMM 230
Cdd:cd05943 273 GTLLQHLKEHILhCDLRPGDRLFYYTTCGWMMwNWLVSGL---AVGA-TIVlydgsPFYP--DTNALWDLADEEGI-TVF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRMLLQQ---------DLSSykfphLQNCVTVGESLLPETLE----NWRAqtGLDIRESYGQTETgLTCMVSkTM 297
Cdd:cd05943 346 GTSAKYLDALEKaglkpaethDLSS-----LRTILSTGSPLKPESFDyvydHIKP--DVLLASISGGTDI-ISCFVG-GN 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 298 KIKPGYMGtAASC----YDVQIIDDKGNVLPpGTEGDIGIrVKPI--RPIGiFSGYVDNPDKTAA--NIRGDFWLLGDRG 369
Cdd:cd05943 417 PLLPVYRG-EIQCrglgMAVEAFDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWNDPDGSRYRAAyfAKYPGVWAHGDWI 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 370 IKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKELQ 449
Cdd:cd05943 493 EITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELR 566
|
490 500 510
....*....|....*....|....*....|....*
gi 815659680 450 QHVKSVTA----PYKYPRKIEFVLNLPKTVTGKIQ 480
Cdd:cd05943 567 KRIRSTIRsalsPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
2-409 |
7.91e-11 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 64.30 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfMPGTIQMKSTD-ILYRLQMSKAKAIVA 80
Cdd:cd05933 9 LTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGI-AVGIYTTNSPEaCQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 81 GDEV-IQEVDTVASECPSLR----IKLLVSEKSCD--GWLNFKKLLNEASTTHHCVETGSQEAS---AIYFTSGTSGLPK 150
Cdd:cd05933 87 ENQKqLQKILQIQDKLPHLKaiiqYKEPLKEKEPNlySWDEFMELGRSIPDEQLDAIISSQKPNqccTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 --MAEH---------------------------SYSSLG-LKAKMDAGWTGL---------QASDIMWTISDT------- 184
Cdd:cd05933 167 gvMLSHdnitwtakaasqhmdlrpatvgqesvvSYLPLShIAAQILDIWLPIkvggqvyfaQPDALKGTLVKTlrevrpt 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 185 -----GWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSsypiKSMMG---APIVYRMLLQQDLSSYK----FPHL 252
Cdd:cd05933 247 afmgvPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNL----KLMGGespSPLFYRLAKKLVFKKVRkalgLDRC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 253 QNCVTVGESLLPETLENWraqTGLDIR--ESYGQTET-GLtcmvsKTMKIKPGYmgTAASCydvqiiddkGNVLPpgteg 329
Cdd:cd05933 323 QKFFTGAAPISRETLEFF---LSLNIPimELYGMSETsGP-----HTISNPQAY--RLLSC---------GKALP----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 330 diGIRVKPIRP----IG--------IFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAND-IINSSGYRIG 395
Cdd:cd05933 379 --GCKTKIHNPdadgIGeicfwgrhVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVP 456
|
490
....*....|....*
gi 815659680 396 PSEVENAL-MEHPAV 409
Cdd:cd05933 457 PVPIEDAVkKELPII 471
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
6-484 |
1.08e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 63.65 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 6 ELSENSQQAANVLSGACglQRGDR-VAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV 84
Cdd:cd17654 21 DLAEKISNLSNFLRKKF--QTEERaIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 85 IQEvdtvasecPSLRIKLLVsekscdgwlNFKKLLNEAStthhcvetgsqeaSAIYFTSGTSGLPK---MAEHSYSS--L 159
Cdd:cd17654 99 DNA--------PLSFTPEHR---------HFNIRTDECL-------------AYVIHTSGTTGTPKivaVPHKCILPniQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 160 GLKAKMDagwtgLQASDIMWTISDTGW---ILNILCSLmepwALGAC-----TFVHLLP-KFDPlvILKTLSSypIKSMM 230
Cdd:cd17654 149 HFRSLFN-----ITSEDILFLTSPLTFdpsVVEIFLSL----SSGATllivpTSVKVLPsKLAD--ILFKRHR--ITVLQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 231 GAPIVYRMLLQQDLSSYKFPHLQN--CVTVGESLLPETLEN--WRAQ-TGLDIRESYGQTETgltCMVSKTMKIK----P 301
Cdd:cd17654 216 ATPTLFRRFGSQSIKSTVLSATSSlrVLALGGEPFPSLVILssWRGKgNRTRIFNIYGITEV---SCWALAYKVPeedsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 302 GYMGTAASCYDVQIIDDKGNvlppgtEGDIGIRVKPIRPIGIFSGYVDNPdktaaniRGDFWLLGDRgIKDEDGYFQFMG 381
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVP-------KGTMRATGDF-VTVKDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 382 RANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDpvrgEVVKAFVVLASqflSHDPEQltKELQQHVKSvtaPYKY 461
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLS---SHAI 426
|
490 500
....*....|....*....|...
gi 815659680 462 PRKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17654 427 PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
4-485 |
2.20e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.10 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMK-------STDILYRLQMSKAK 76
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 77 AIVAGDEVIQEVDTVASecpSLRIKLLVSekscdgWLNFKkLLNEASTThhcVETGSQEASA-IYFTSGTSGLPK----- 150
Cdd:PRK09192 131 AIITPDELLPWVNEATH---GNPLLHVLS------HAWFK-ALPEADVA---LPRPTPDDIAyLQYSSGSTRFPRgviit 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 151 ----MAE-HSYSSLGLKakmdagwtgLQASD--IMW-----TISDTGWILNILCSLMEpwalgactfVHLLPKFD----P 214
Cdd:PRK09192 198 hralMANlRAISHDGLK---------VRPGDrcVSWlpfyhDMGLVGFLLTPVATQLS---------VDYLPTRDfarrP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 215 LVILK-------TLSSYPiksMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR---AQTGLDIRE---S 281
Cdd:PRK09192 260 LQWLDlisrnrgTISYSP---PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAeafAPAGFDDKAfmpS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 282 YGQTETGL------------------TCMVSKTMKIKPGYMGTAAS----C------YDVQIIDDKGNVLPPGTEGDIGI 333
Cdd:PRK09192 337 YGLAEATLavsfsplgsgivveevdrDRLEYQGKAVAPGAETRRVRtfvnCgkalpgHEIEIRNEAGMPLPERVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 334 RvKPirpiGIFSGYVDNPDkTAANIRGDFWL-LGDRGIKdEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVV-- 410
Cdd:PRK09192 417 R-GP----SLMSGYFRDEE-SQDVLAADGWLdTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsg 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 411 ETAVISSPDPvRGEVVkafVVLASQFLShDPE---QLTKELQQHVKSVTApykYPRKIEFV--LNLPKTVTGKIQRAKLR 485
Cdd:PRK09192 490 DAAAFSIAQE-NGEKI---VLLVQCRIS-DEErrgQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
34-496 |
3.96e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 34 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQE------VDTVASECPSLRIKLLVSEK 107
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 108 SCD--------GWLNFkklLNEASTTHhcvETGSQEASAIY----------FTSGTSGLPKMAEHSYSSlGLKAKMDaGW 169
Cdd:PLN03051 81 PVAvplreqdlSWCDF---LGVAAAQG---SVGGNEYSPVYapvesvtnilFSSGTTGEPKAIPWTHLS-PLRCASD-GW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 170 TGL--QASDIMWTISDTGWILN-ILcsLMEPWALGACTFVH----LLPKFDPLV------ILKTlssypIKSMMGApivY 236
Cdd:PLN03051 153 AHMdiQPGDVVCWPTNLGWMMGpWL--LYSAFLNGATLALYggapLGRGFGKFVqdagvtVLGL-----VPSIVKA---W 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 237 RMLLQQDLSSYKFPHLQNCVTVGESLLPET---LENWRAQTGlDIRESYGQTETGLTCMVSKTMKIK-PGYMGTAASCYD 312
Cdd:PLN03051 223 RHTGAFAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 313 VQIIDDKGNVLPPGTE--GDIGIRVkpirPIGIFSGYVDNPDKTAANIRG---------DFWLLGDRGIKDEDGYFQFMG 381
Cdd:PLN03051 302 FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpmygskgmPLRRHGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 382 RANDIINSSGYRIGPSEVENALME-HPAVVETAVISSPDPVRGE----VVKAFVVLASQFLSHDPEQLTKELQQHVKSVT 456
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 815659680 457 APYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK-MSGKAR 496
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRSK 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4-422 |
1.23e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 60.17 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstDILyrlqmskakaivagde 83
Cdd:cd05910 5 FRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV-----------PVL---------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 viqeVDtvasecPSLRIKllvsekscdgwlNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLglKA 163
Cdd:cd05910 57 ----ID------PGMGRK------------NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTF--AA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWT--GLQASDI-MWTISdtgwilniLCSLMEPwALGACTFV----HLLP-KFDPLVILKTLSSYPIKSMMGAPIV 235
Cdd:cd05910 113 QIDALRQlyGIRPGEVdLATFP--------LFALFGP-ALGLTSVIpdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 236 YRML----LQQDLssyKFPHLQNCVTVGESLLPETLENWRA--QTGLDIRESYGQTETGLTCMV-------SKTMKIKPG 302
Cdd:cd05910 184 LERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSIgsrellaTTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 303 Y---MGTAASCYDVQIID---------DKGNVLPPGTEGDI---GIRVKPirpigifsGYVDNPDKTAA----NIRGDFW 363
Cdd:cd05910 261 AgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEItvtGPTVTP--------TYVNRPVATALakidDNSEGFW 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 364 -LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 422
Cdd:cd05910 333 hRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGC 392
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
133-485 |
1.94e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 133 SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLlpkF 212
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSL------------LANVEQIKTIADFTPNDRFMSALPLFHSFGLT--VGL---F 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 DPLVILKTLSSYPiksmmgAPIVYRML--LQQD------------LSSY-KFPH------LQNCVTVGESLLPETLENWR 271
Cdd:PRK08043 427 TPLLTGAEVFLYP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 272 AQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIddkgNVlpPGTEGdiGIRVKpIRPIGIFSGY--VD 349
Cdd:PRK08043 501 DKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL----SV--PGIEQ--GGRLQ-LKGPNIMNGYlrVE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 350 NPDK----TAANIRGDF---WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN-ALMEHPAVVETAVISSpDP 420
Cdd:PRK08043 572 KPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DA 650
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815659680 421 VRGEvvkAFVVLASqflshDPEqLTKE-LQQHVKSVTAP-YKYPRKIEFVLNLPKTVTGKIQRAKLR 485
Cdd:PRK08043 651 SKGE---ALVLFTT-----DSE-LTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
138-486 |
6.42e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.78 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 138 AIYFTSGTSGLPKMAEHSYSSLGLKAKmdagwtglQASDIMWTISDTgwilNILCSLmePW--ALG--ACTFVHLLPKF- 212
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNIE--------QISDVFNLRNDD----VILSSL--PFfhSFGltVTLWLPLLEGIk 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 213 -----DPL---VILKTLSSYPIKSMMGAPIVYRMLLQQD-LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYG 283
Cdd:PRK08633 852 vvyhpDPTdalGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 284 QTETGLTCMVSKTMKIKPGYM---------------GTAascydVQIID-DKGNVLPPGTEGDIgirvkPIRPIGIFSGY 347
Cdd:PRK08633 932 ATETSPVASVNLPDVLAADFKrqtgskegsvgmplpGVA-----VRIVDpETFEELPPGEDGLI-----LIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 348 VDNPDKTA---ANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALME--HPAVVETAVISSPDPV 421
Cdd:PRK08633 1002 LGDPEKTAeviKDIDGIGWYVtGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815659680 422 RGEVVkafVVLASQflshdPEQLTKELQQHVKSVTAP--YKyPRKIEFVLNLPKTVTGKIQRAKLRD 486
Cdd:PRK08633 1082 KGEKL---VVLHTC-----GAEDVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
256-486 |
4.64e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 55.30 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 256 VTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID--DKG-NVLPPGTEGDIG 332
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVC 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 333 IRVKpirpiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSEVENALMEHPAVV 410
Cdd:cd05927 360 IRGP-----NVFSGYYKDPEKTAEALDEDGWLHtGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 411 ETAV-----------ISSPDPvrgEVVKAFvvLASQFL-SHDPEQLTK--ELQQHV---------KSVTAPYKYPRKIEF 467
Cdd:cd05927 435 QIFVygdslksflvaIVVPDP---DVLKEW--AASKGGgTGSFEELCKnpEVKKAIledlvrlgkENGLKGFEQVKAIHL 509
|
250 260
....*....|....*....|....*
gi 815659680 468 VLNLPK------TVTGKIQRAKLRD 486
Cdd:cd05927 510 EPEPFSvengllTPTFKLKRPQLKK 534
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
363-480 |
8.96e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 51.33 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 363 WLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPE 442
Cdd:PRK03584 500 WRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA------EGV 573
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 815659680 443 QLTKELQQHVKSV----TAPYKYPRKIEFVLNLPKTVTGKIQ 480
Cdd:PRK03584 574 TLDDALRARIRTTirtnLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
262-428 |
2.11e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 262 LLPETLENWRAQTGLDIRESYGQTETglTCMVSKTMK--IKPGYMGTAASCYDVQIID---------DKgnvlpPGTEGD 330
Cdd:PLN02736 388 LSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEgdNLSGHVGSPNPACEVKLVDvpemnytseDQ-----PYPRGE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 331 IGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSEVENALMEHPA 408
Cdd:PLN02736 461 ICVR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENVYAKCKF 535
|
170 180 190
....*....|....*....|....*....|.
gi 815659680 409 VVETAV-----------ISSPDPvrgEVVKA 428
Cdd:PLN02736 536 VAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
338-485 |
7.73e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 338 IRPIGIFSGYVDnpdktAANIRGDFWL-LGDRGIKDEDGyFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIS 416
Cdd:PRK05851 377 IRGASMMSGYLG-----QAPIDPDDWFpTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815659680 417 SPDPVRGevVKAFVVLASQFLSHDPEQLTKELQQHVKSVTApyKYPRKIEFVL--NLPKTVTGKIQRAKLR 485
Cdd:PRK05851 451 VGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
203-484 |
1.17e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.43 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 203 CTFVHLLPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSykfphLQ----NCVTVGeslLPETLENWRAQTGLDI 278
Cdd:cd17647 201 ATVTHLTPAMGQL--LTAQATTPFPKLHHAFFVGDILTKRDCLR-----LQtlaeNVRIVN---MYGTTETQRAVSYFEV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 279 ReSYGQTETGLtcmvsKTMK-IKPGYMGTaascYDVQII----DDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDK 353
Cdd:cd17647 271 P-SRSSDPTFL-----KNLKdVMPAGRGM----LNVQLLvvnrNDRTQICGIGEVGEIYVRAG-----GLAEGYRGLPEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 354 TAANIRGD---------------------FWL--------LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALM 404
Cdd:cd17647 336 NKEKFVNNwfvepdhwnyldkdnnepwrqFWLgprdrlyrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 405 EHPAVVET------------AVIS--SPDPVRGEVVKAFVVLASQFLSHDP--------EQLTKELQQHVKSVTAPYKYP 462
Cdd:cd17647 416 QHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
330 340
....*....|....*....|..
gi 815659680 463 RKIEFVLNLPKTVTGKIQRAKL 484
Cdd:cd17647 496 SLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
256-489 |
4.03e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.88 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 256 VTVGESLLPETLENWRAQTGLDIRESYGQTET-GLT--------CMVsktmkikpGYMGTAASCYDVQI-------IDDK 319
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlGPTtlgfpdemCML--------GTVGAPAVYNELRLeevpemgYDPL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 320 GNvlPPgtEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSE 398
Cdd:PLN02430 461 GE--PP--RGEICVRGKCL-----FSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEY 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 399 VENALMEHPAVVETAVISspDPVRGEVVkAFVVLasqflshDPEQLTK--ELQQHVKSVTAPYKYPRKIEFVLNLPKTVT 476
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVP-------NEENTNKwaKDNGFTGSFEELCSLPELKEHILSELKSTA 601
|
250
....*....|...
gi 815659680 477 gkiQRAKLRDKEW 489
Cdd:PLN02430 602 ---EKNKLRGFEY 611
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2-489 |
4.90e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 42.55 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 2 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAG---LIFMPGTIQMKSTDILYRLQmskakai 78
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGarvLPLNPQLPQPLLEELLPSLT------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 79 vagdeviqeVDTVASECPSLRIKLLVSekscdgwlnfkKLLNEASTTHHCVETGSQEASAIyFTSGTSGLPKMAEHSY-- 156
Cdd:PRK09029 101 ---------LDFALVLEGENTFSALTS-----------LHLQLVEGAHAVAWQPQRLATMT-LTSGSTGLPKAAVHTAqa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 157 ---SSLGLKAKMDagwtgLQASDimwtisdtGWILnilcSLmepwalgactfvhllpkfdPL--VilktlssypikSMMG 231
Cdd:PRK09029 160 hlaSAEGVLSLMP-----FTAQD--------SWLL----SL-------------------PLfhV-----------SGQG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 232 apIVYRMLLQ---------QDLSSykfpHLQNCVTVgeSLLPeT-----LENWRAQTGLD--------IRESYGQ--TET 287
Cdd:PRK09029 193 --IVWRWLYAgatlvvrdkQPLEQ----ALAGCTHA--SLVP-TqlwrlLDNRSEPLSLKavllggaaIPVELTEqaEQQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 288 GLTCMVsktmkikpGY-MGTAASCYDVQIIDDKGNV-LP-PGTE-----GDIGIRVKpirpiGIFSGYvdnpdktaanir 359
Cdd:PRK09029 264 GIRCWC--------GYgLTEMASTVCAKRADGLAGVgSPlPGREvklvdGEIWLRGA-----SLALGY------------ 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 360 gdfWLlgDRGIK---DEDGYFQ-------------FMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD---- 419
Cdd:PRK09029 319 ---WR--QGQLVplvNDEGWFAtrdrgewqngeltILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaefg 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815659680 420 --PVrgevvkAFVVLASqflshdpEQLTKELQQHVKSVTAPYKYPrkIEFVLnLPKTV-TG--KIQRAKLrdKEW 489
Cdd:PRK09029 394 qrPV------AVVESDS-------EAAVVNLAEWLQDKLARFQQP--VAYYL-LPPELkNGgiKISRQAL--KEW 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-485 |
8.68e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.08 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 4 FRELSENSQQAANVLSGACGLqrGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTdilyRLQMSKAKAIVAgDE 83
Cdd:PRK05691 43 YRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESAR----RHHQERLLSIIA-DA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 84 VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 163
Cdd:PRK05691 116 EPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 164 KMDAGWTGLQASD----IMWT--ISDTGWILNIL--------CSLMEPwalgactfVHLLPKfdPLVILKTLSSYPIKSM 229
Cdd:PRK05691 196 QLIRHGFGIDLNPddviVSWLplYHDMGLIGGLLqpifsgvpCVLMSP--------AYFLER--PLRWLEAISEYGGTIS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 230 MGAPIVYRMLLQQdlssykfphlqncvtVGESLLPE-TLENWR-AQTGLD-IRE----------------------SYGQ 284
Cdd:PRK05691 266 GGPDFAYRLCSER---------------VSESALERlDLSRWRvAYSGSEpIRQdslerfaekfaacgfdpdsffaSYGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 285 TETglTCMVSKTMK------------------IKPGYMGTAASC------YDVQIID-DKGNVLPPGTEGDIGiRVKPir 339
Cdd:PRK05691 331 AEA--TLFVSGGRRgqgipaleldaealarnrAEPGTGSVLMSCgrsqpgHAVLIVDpQSLEVLGDNRVGEIW-ASGP-- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 340 piGIFSGYVDNPDKTA---ANIRGDFWL-LGDRGIKdEDGYFQFMGRANDIINSSGYRIGPSEVENalmehpaVVETAVi 415
Cdd:PRK05691 406 --SIAHGYWRNPEASAktfVEHDGRTWLrTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEK-------TVEREV- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815659680 416 sspDPVRGEVVKAFVV---------LASQF-----LSHDPEQLTKELQQHVKSVtapYKYPRKIEFVLN---LPKTVTGK 478
Cdd:PRK05691 475 ---EVVRKGRVAAFAVnhqgeegigIAAEIsrsvqKILPPQALIKSIRQAVAEA---CQEAPSVVLLLNpgaLPKTSSGK 548
|
....*..
gi 815659680 479 IQRAKLR 485
Cdd:PRK05691 549 LQRSACR 555
|
|
| |
